Last updated: Thursday, July 2, 2009 4:03 PM

Supplementary Material

Structural Biology of the Purine Biosynthesis Pathway by Yang Zhang, Mariya Morar and Steven E. Ealick Cell. Mol. Life Sci. 65:3699-3724 (2008). PubMed

Please notify Steve Ealick (see3@cornell.edu) if you have any corrections or updates to this list.

References are listed at the bottom and have clickable live links to their PubMed or other electronic entry.

Appendix 1: PurF Structures

Organism	PDB Code	Ligands	Reference
E. coli	1ECF	PIN	[1]
E. coli	1ECG	ONL, PIN	[2]
E. coli	1ECC	ONL, PCP, Mn	[3]
E. coli	1ECB	GMP, Mg	[3]
E. coli	1ECJ	AMP	[1]
B. subtilis	1GPH	AMP, Fe₄S₄	[4]
B. subtilis	1AO0	GMP, ADP, Mg, Fe₄S₄	[5]

Appendix 2: PurD Structures

Organism	PDB Code	Ligands	Reference
E. coli	1GSO	sulfate	[6]
T. thermophilus	2IP4	sulfate	TBP
H. sapiens	2QK4	ATP, sulfate, glycerol, chloride	TBP
G. kaustophilus	2YRW	phosphate	TBP
G. kaustophilus	2YS6	AMP, glycine	TBP
G. kaustophilus	2YS7	-	TBP
G. kaustophilus	2YRX	AMP, phosphate	TBP
A. aeolicus	2YYA	-	TBP
A. aeolicus	2YW2	ATP, phosphate	TBP

Appendix 3: PurN and PurT Structures

Organism	PDB Code	Ligands	Reference
PurN
E. coli	1CDE	GAR, THF analog	[7]
E. coli	1GRC	phosphate	[8]
E. coli	1GAR	inhibitor	[9]
E. coli	1C2T	GAR, THF analog	[10]
E. coli	1C3E	GAR, THF analog	[10]
H. sapiens	1JKX	inhibitor	[11]
H. sapiens	1MEN	GAR	[12]
H. sapiens	1MEJ	glycerol, phosphate	[12]
H. sapiens	1MEO	phosphate, sulfate	[12]
H. sapiens	1NJS	inhibitor, phosphate	[13]
H. sapiens	1ZLX	glycerol	[14]
H. sapiens	1ZLY	GAR analog, THF analog	[14]
H. sapiens	1RBZ	THF analog	TBP
H. sapiens	1RC1	THF analog, phosphate	TBP
H. sapiens	1RC0	THF analog	TBP
H. sapiens	1RBY	GAR, THF analog	TBP
H. sapiens	1RBQ	THF analog, phosphate	TBP
H. sapiens	1RBM	THF analog, phosphate	TBP
A. aeolicus	2YWR	Co, Mg	TBP
PurT
E. coli	1KJ8	GAR, ATP, MPO, ethanediol, Mg, Na, Cl	[15]
E. coli	1KJQ	ADP, MPO, ethanediol, Mg, Na, Cl	[15]
E. coli	1KJ9	ATP, MPO, ethanediol, Mg, Na, Cl	[15]
E. coli	1KJI	ATP analog, MPO, ethanediol, Mg, Na, Cl	[15]
E. coli	1KJJ	ATP analog, MPO, Mg, Na, Cl	[15]
E. coli	1EZ1	ATP analog, GAR, MPO, acetate, Mg, Na	[16]
E. coli	1EYZ	ATP analog, MPO, Mg, Na, Cl	[16]

Appendix 4: PurL, PurS and PurLQS Structures

Organism	PDB Code	Ligands	Reference
lgPurL
S. typhimurium	1T3T	Gln-thioester, ADP, sulfate, Mg	[17]
smPurL
T. maritima	2HS3	FGAR, phosphate	[18]
T. maritima	2HRU	ADP, Mg	[18]
T. maritima	2HRY	AMPPCP, Mg, phosphate	[18]
T. maritima	2HS0	ATP, Mg	[18]
T. maritima	2HS4	AMPPCP, FGAR, Mg, phosphate	[18]
T. maritima	1VK3		[19]
PurS
B. subtilis	1TWJ	-	[20]
T. thermophilis	2CUW	-	TBP
T. thermophilis	2DGB		TBP
T. maritima	1VQ3		[21]
B. subtilis	1T4A		[20]
M. jannaschii	2YX5		TBP
M. thermoautotrophicum	1GTD		[22]
PurLQS
S. typhimurium	3D54	Gln-thioester	[23]

Appendix 3: PurM Structures

Organism	PDB Code	Ligands	Reference
E. coli	1CLI	sulfate	[24]
B. anthracis	2BTU	-	TBP

Appendix 6: PurE and PurK Structures

Organism	PDB Code	Ligands	Reference
PurE
E. coli	1D7A	AIR	[25]
E. coli	1QCZ	-	[25]
E. coli	2ATE	nitroAIR	[26]
E. coli	2NSH	nitroAIR	[26]
E. coli	2NSJ	CAIR	[26]
E. coli	2NSL	CAIR	[26]
A. aceti	1U11	-	[27]
A. aceti	2FW1	acetic acid	[28]
A. aceti	2FW6	citric acid	[28]
A. aceti	2FW7	-	[28]
A. aceti	2FW8	-	[28]
A. aceti	2FW9	sulfate	[28]
A. aceti	2FWA	-	[28]
A. aceti	2FWB	-	[28]
A. aceti	2FWI	AIR	[28]
A. aceti	2FWJ	AIR	[28]
A. aceti	2FWP	citric acid, ICR	[28]
PurCE
H. sapiens	2H31	CO₂	[29]
PurK
E. coli	1B6R	sulfate	[30]
E. coli	1B6S	ADP, Mg	[30]

Appendix 7: PurC Structures

Organism	PDB Code	Ligands	Reference
PurC
S. cerevisiae	1A48	sulfate, acetyl group	[31]
S. cerevisiae	1OBD	ATP, AMP, acetyl group, sulfate, Mg	[32]
S. cerevisiae	1OBG	AMP, sulfate, Mg	[32]
S. cerevisiae	2CNQ	AICAR, ADP, AMP, acetyl group, sulfate, Mg, succinic acid	TBP
S. cerevisiae	2CNU	Asp, acetyl group, sulfate	TBP
S. cerevisiae	2CNV	SAICAR, Asp, acetyl group, sulfate	TBP
T. maritima	1KUT	-	[33]
E. coli	2GQR	ADP, Mg, formic acid, Mg	[34]
E. coli	2GQS	CAIR, ADP	[34]
M. jannaschii	2YZL	ADP, sulfate	TBP
M. jannaschii	2Z02	ATP, citric acid, sulfate	TBP
G. kaustophilus	2YWV	ADP, sulfate, Mg	TBP
PurCE
H. sapiens	2H31	CO₂	[29]

Appendix 8: PurB Structures

Organism	PDB Code	Ligands	Reference
T. maritima	1C3C	-	[35]
T. maritima	1C3U	sulfate	[35]
P. aerophilum	1F1O	-	[36]
P. aerophilum	1DOF	-	[36]
C. elegans	1YIS	sulfate	TBP
H. sapiens	2J91	AMP, Cl, glycerol	TBP
P. vivax	2HVG	sulfate	[37]
P. vivax	2QGA	AMP, sulfate, Ca	TBP
B. anthracis	2PFM	malonate	TBP
E. coli	2PTQ	fumarate, AMP	[38]
E. coli	2PTR	adenylsuccinate	[38]
E. coli	2PTS	-	[38]
H. sapiens	2VD6	adenylsuccinate, fumarate, AMP, Cl, glycerol	TBP

Appendix 9: PurHJ, PurP and PurO Structures

Organism	PDB Code	Ligands	Reference
PurHj
G. gallus	1G8M	GMP, K	[39]
G. gallus	1M9N	XMP, AICAR, K	[40]
G. gallus	1OZ0	inhibitor, K, phosphate	[41]
G. gallus	1THZ	inhibitor, K	[42]
G. gallus	2B1I	inhibitor, K	[43]
G. gallus	2B1G	inhibitor, K, phosphate	[43]
G. gallus	2IU0	inhibitor, K	[43]
G. gallus	2IU3	inhibitor, K	[43]
H. sapiens	1P4R	inhibitor, XMP, AICAR, K	[44]
H. sapiens	1PL0	inhibitor, XMP, AICAR, K	[44]
H. sapiens	1PKX	XMP, K	[45]
T. maritima	1ZCZ	K, tetraethylene glycol	[49]
PurP
M. jannaschii	2R7K	AICAR, AMPPCP, Cl, sulfate	[46]
M. jannaschii	2R7L	AICAR, ATP, Cl, sulfate	[46]
M. jannaschii	2R7M	AMP, Cl, sulfate	[46]
M. jannaschii	2R7N	FAICAR, ADP, Cl, sulfate	[46]
P. furiosus	2R84	AICAR, AMP, MPD, Cl, Na	[46]
P. furiosus	2R85	AMP, MPD, Cl, Na	[46]
P. furiosus	2R86	ATP, phosphate, MPD, Na	[46]
P. furiosus	2R87	ADP, phosphate	[46]
T. kodakaraensis	2PBZ	ATP	TBP
PurO
M. thermoautotrophicum	1KUU	-	[47]
M. thermoautotrophicum	2NTK	IMP	[48]
M. thermoautotrophicum	2NTL	AICAR	[48]
M. thermoautotrophicum	2NTM	-	[48]

[1]       Muchmore, C.R., Krahn, J.M., Kim, J.H., Zalkin, H. and Smith, J.L. (1998). Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Protein Sci. 7, 39-51.

[2]       Kim, J.H., Krahn, J.M., Tomchick, D.R., Smith, J.L. and Zalkin, H. (1996). Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271, 15549-15557.

[3]       Krahn, J.M., Kim, J.H., Burns, M.R., Parry, R.J., Zalkin, H. and Smith, J.L. (1997). Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry 36, 11061-11068.

[4]       Smith, J.L., Zaluzec, E.J., Wery, J.P., Niu, L., Switzer, R.L., Zalkin, H. and Satow, Y. (1994). Structure of the allosteric regulatory enzyme of purine biosynthesis. Science 264, 1427-1433.

[5]       Chen, S., Tomchick, D.R., Wolle, D., Hu, P., Smith, J.L., Switzer, R.L. and Zalkin, H. (1997). Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry 36, 10718-10726.

[6]       Wang, W., Kappock, T.J., Stubbe, J. and Ealick, S.E. (1998). X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. Biochemistry 37, 15647-15662.

[7]       Almassy, R.J., Janson, C.A., Kan, C.C. and Hostomska, Z. (1992). Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. Proc. Natl. Acad. Sci. U. S. A. 89, 6114-6118.

[8]       Chen, P., Schulze-Gahmen, U., Stura, E.A., Inglese, J., Johnson, D.L., Marolewski, A., Benkovic, S.J. and Wilson, I.A. (1992). Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 Å resolution. A target enzyme for chemotherapy. J. Mol. Biol. 227, 283-292.

[9]       Klein, C., Chen, P., Arevalo, J.H., Stura, E.A., Marolewski, A., Warren, M.S., Benkovic, S.J. and Wilson, I.A. (1995). Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 Å resolution. J. Mol. Biol. 249, 153-175.

[10]     Greasley, S.E., Yamashita, M.M., Cai, H., Benkovic, S.J., Boger, D.L. and Wilson, I.A. (1999). New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with β-GAR and 10-formyl-5,8,10-trideazafolic acid. Biochemistry 38, 16783-16793.

[11]     Greasley, S.E., Marsilje, T.H., Cai, H., Baker, S., Benkovic, S.J., Boger, D.L. and Wilson, I.A. (2001). Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase. Biochemistry 40, 13538-13547.

[12]     Zhang, Y., Desharnais, J., Greasley, S.E., Beardsley, G.P., Boger, D.L. and Wilson, I.A. (2002). Crystal structures of human GAR Tfase at low and high pH and with substrate β-GAR. Biochemistry 41, 14206-14215.

[13]     Zhang, Y., Desharnais, J., Marsilje, T.H., Li, C., Hedrick, M.P., Gooljarsingh, L.T., Tavassoli, A., Benkovic, S.J., Olson, A.J., Boger, D.L. and Wilson, I.A. (2003). Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry 42, 6043-6056.

[14]     Dahms, T.E., Sainz, G., Giroux, E.L., Caperelli, C.A. and Smith, J.L. (2005). The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry 44, 9841-9850.

[15]     Thoden, J.B., Firestine, S.M., Benkovic, S.J. and Holden, H.M. (2002). PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site. J. Biol. Chem. 277, 23898-23908.

[16]     Thoden, J.B., Firestine, S., Nixon, A., Benkovic, S.J. and Holden, H.M. (2000). Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase. Biochemistry 39, 8791-8802.

[17]     Anand, R., Hoskins, A.A., Stubbe, J. and Ealick, S.E. (2004). Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. Biochemistry 43, 10328-10342.

[18]     Morar, M., Anand, R., Hoskins, A.A., Stubbe, J. and Ealick, S.E. (2006). Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. Biochemistry 45, 14880-14895.

[19]     Mathews, II, Krishna, S.S., Schwarzenbacher, R., McMullan, D., Abdubek, P., Ambing, E., Canaves, J.M., Chiu, H.J., Deacon, A.M., DiDonato, M., Elsliger, M.A., Godzik, A., Grittini, C., Grzechnik, S.K., Hale, J., Hampton, E., Han, G.W., Haugen, J., Jaroszewski, L., Klock, H.E., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., Levin, I., Miller, M.D., Moy, K., Nigoghossian, E., Paulsen, J., Quijano, K., Reyes, R., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J. and Wilson, I.A. (2006). Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 Å resolution. Proteins 63, 1106-1111.

[20]     Anand, R., Hoskins, A.A., Bennett, E.M., Sintchak, M.D., Stubbe, J. and Ealick, S.E. (2004). A model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex. Biochemistry 43, 10343-10352.

[21]     Mathews, II, Krishna, S.S., Schwarzenbacher, R., McMullan, D., Jaroszewski, L., Miller, M.D., Abdubek, P., Agarwalla, S., Ambing, E., Axelrod, H.L., Canaves, J.M., Carlton, D., Chiu, H.J., Clayton, T., DiDonato, M., Duan, L., Elsliger, M.A., Grzechnik, S.K., Hale, J., Hampton, E., Haugen, J., Jin, K.K., Klock, H.E., Koesema, E., Kovarik, J.S., Kreusch, A., Kuhn, P., Levin, I., Morse, A.T., Nigoghossian, E., Okach, L., Oommachen, S., Paulsen, J., Quijano, K., Reyes, R., Rife, C.L., Spraggon, G., Stevens, R.C., van den Bedem, H., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. (2006). Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) from Thermotoga maritima at 1.90 Å resolution. Proteins 65, 249-254.

[22] Batra, R., Christendat, D., Edwards, A., Arrowsmith, C. and Tong, L. (2002). Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase. Proteins 49, 285-288.

[23] Morar, M., Hoskins, A.A., Stubbe, J. and Ealick, S.E. (2008). Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima: Structural Insights into Complex Formation. Biochemistry 47, 7816-7830.

[24] Li, C., Kappock, T.J., Stubbe, J., Weaver, T.M. and Ealick, S.E. (1999). X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 Å resolution. Structure 7, 1155-1166.

[25] Mathews, II, Kappock, T.J., Stubbe, J. and Ealick, S.E. (1999). Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway. Structure 7, 1395-1406.

[26] Hoskins, A.A., Morar, M., Kappock, T.J., Mathews, II, Zaugg, J.B., Barder, T.E., Peng, P., Okamoto, A., Ealick, S.E. and Stubbe, J. (2007). N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis. Biochemistry 46, 2842-2855.

[27] Settembre, E.C., Chittuluru, J.R., Mill, C.P., Kappock, T.J. and Ealick, S.E. (2004). Acidophilic adaptations in the structure of Acetobacter aceti N⁵-carboxyaminoimidazole ribonucleotide mutase (PurE). Acta Crystallogr. D 60, 1753-1760.

[28] Constantine, C.Z., Starks, C.M., Mill, C.P., Ransome, A.E., Karpowicz, S.J., Francois, J.A., Goodman, R.A. and Kappock, T.J. (2006). Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti. Biochemistry 45, 8193-8208.

[29] Li, S.X., Tong, Y.P., Xie, X.C., Wang, Q.H., Zhou, H.N., Han, Y., Zhang, Z.Y., Gao, W., Li, S.G., Zhang, X.C. and Bi, R.C. (2007). Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. J. Mol. Biol. 366, 1603-1614.

[30] Thoden, J.B., Kappock, T.J., Stubbe, J. and Holden, H.M. (1999). Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily. Biochemistry 38, 15480-15492.

[31] Levdikov, V.M., Barynin, V.V., Grebenko, A.I., Melik-Adamyan, W.R., Lamzin, V.S. and Wilson, K.S. (1998). The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis. Structure 6, 363-376.

[32] Antopyuk, S.V., Grebenko, A.I., Levdikov, V.M., Urusova, D.V., Melik-Adamyan, V.R., Lamzin, V.S. and Wilson, K.S. (2001). X-ray study of SAICAR synthase complexes with adenosinetriphosphate. Kristallografiya 46, 687-691.

[33] Zhang, R., Skarina, T., Evdokimova, E., Edwards, A., Savchenko, A., Laskowski, R., Cuff, M.E. and Joachimiak, A. (2006). Structure of SAICAR synthase from Thermotoga maritima at 2.2 Å reveals an unusual covalent dimer. Acta Crystallogr. F 62, 335-339.

[34] Ginder, N.D., Binkowski, D.J., Fromm, H.J. and Honzatko, R.B. (2006). Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase. J. Biol. Chem. 281, 20680-20688.

[35] Toth, E.A. and Yeates, T.O. (2000). The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway. Structure 8, 163-174.

[36] Toth, E.A., Worby, C., Dixon, J.E., Goedken, E.R., Marqusee, S. and Yeates, T.O. (2000). The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. J. Mol. Biol. 301, 433-450.

[37] Vedadi, M., Lew, J., Artz, J., Amani, M., Zhao, Y., Dong, A., Wasney, G.A., Gao, M., Hills, T., Brokx, S., Qiu, W., Sharma, S., Diassiti, A., Alam, Z., Melone, M., Mulichak, A., Wernimont, A., Bray, J., Loppnau, P., Plotnikova, O., Newberry, K., Sundararajan, E., Houston, S., Walker, J., Tempel, W., Bochkarev, A., Kozieradzki, I., Edwards, A., Arrowsmith, C., Roos, D., Kain, K. and Hui, R. (2007). Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151, 100-110.

[38] Tsai, M., Koo, J., Yip, P., Colman, R.F., Segall, M.L. and Howell, P.L. (2007). Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism. J. Mol. Biol. 370, 541-554.

[39] Greasley, S.E., Horton, P., Ramcharan, J., Beardsley, G.P., Benkovic, S.J. and Wilson, I.A. (2001). Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis. Nat. Struct. Biol. 8, 402-406.

[40] Wolan, D.W., Greasley, S.E., Beardsley, G.P. and Wilson, I.A. (2002). Structural insights into the avian AICAR transformylase mechanism. Biochemistry 41, 15505-15513.

[41] Wolan, D.W., Greasley, S.E., Wall, M.J., Benkovic, S.J. and Wilson, I.A. (2003). Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor β-DADF identifies the folate binding site. Biochemistry 42, 10904-10914.

[42] Xu, L., Li, C., Olson, A.J. and Wilson, I.A. (2004). Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening. J. Biol. Chem. 279, 50555-50565.

[43] Xu, L., Chong, Y., Hwang, I., D'Onofrio, A., Amore, K., Beardsley, G.P., Li, C., Olson, A.J., Boger, D.L. and Wilson, I.A. (2007). Structure-based design, synthesis, evaluation, and crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase. J. Biol. Chem. 282, 13033-13046.

[44] Cheong, C.G., Wolan, D.W., Greasley, S.E., Horton, P.A., Beardsley, G.P. and Wilson, I.A. (2004). Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates. J. Biol. Chem. 279, 18034-18045.

[45] Wolan, D.W., Cheong, C.G., Greasley, S.E. and Wilson, I.A. (2004). Structural insights into the H. sapiens and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor. Biochemistry 43, 1171-1183.

[46] Zhang, Y., White, R.H. and Ealick, S.E. (2008). Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii. Biochemistry 47, 205-217.

[47] Saridakis, V., Christendat, D., Thygesen, A., Arrowsmith, C.H., Edwards, A.M. and Pai, E.F. (2002). Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold. Proteins 48, 141-143.

[48] Kang, Y.N., Tran, A., White, R.H. and Ealick, S.E. (2007). A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase. Biochemistry 46, 5050-5062.

[49] Axelrod, H. L., McMullan, D., Krishna, S. S., Miller, M. D., Elsliger, M. A., Abdubek, P., Ambing, E., Astakhova, T., Carlton, D., Chiu, H. J., Clayton, T., Duan, L., Feuerhelm, J., Grzechnik, S. K., Hale, J., Han, G. W., Haugen, J., Jaroszewski, L., Jin, K. K., Klock, H. E., Knuth, M. W., Koesema, E., Morse, A. T., Nigoghossian, E., Okach, L., Oommachen, S., Paulsen, J., Quijano, K., Reyes, R., Rife, C. L., van den Bedem, H., Weekes, D., White, A., Wolf, G., Xu, Q., Hodgson, K. O., Wooley, J., Deacon, A. M., Godzik, A., Lesley, S. A., and Wilson, I. A. (2008) Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 Å resolution, Proteins 71, 1042-1049.