Steve Ealick's Research Group

Christopher Jurgenson

Email: ctj8@cornell.edu

BS: Biochemistry, 1998, Indiana University

MS: Chemistry, 2002, Seton Hall University

MS: Chemistry, 2005, Cornell University

Experience:

Research chemist for Merck Pharmaceuticals,1998-2003
Sixth year chemistry grad student

Current Projects:

Structure solution of enzymes involved in a novel prokaryotic sulfur transfer reaction and elucidation of the biochemical mechanism utilizing this structural information
Investigation of the thiamin biosynthetic pathway in eukaryotes.

Finished project:
Model refinement of a purine nucleoside phosphorylase from the organism Thermotoga maritima in collaboration with the Joint Center for Structural Genomics and the Stanford Linear Accelerator Center.

Publications

Jurgenson CT, Chatterjee A, Begley TP and Ealick SE. Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae. Biochemistry 45:11061-11070 (2006). PDB code: 2GJC PubMed.

Chatterjee A, Jurgenson CT, Schroeder FC, Ealick SE, and Begley TP. Thiamin Biosynthesis in Eukaryotes: Characterization of the Enzyme-Bound Product of Thiazole Synthase from Saccharomyces cerevisiae and Its Implications in Thiazole Biosynthesis. J. Am. Chem. Soc. 128:7158-7159 (2006). PubMed

Chatterjee A, Jurgenson CT, Schroeder FC, Ealick SE, and Begley TP. Biosynthesis of the Thiamin Thiazole in Eukaryotes: The Conversion of NAD to an Advanced Intermediate. J. Am. Chem. Soc. 129:126-134 (2007). PubMed

Chatterjee, A, Schroeder FC, Jurgenson CT, Ealick SE, and Begley TP. Biosynthesis of the Thiamin-Thiazole in Eukaryotes: Identification of a Thiazole Tautomer Intermediate. J. Am. Chem. Soc. Accepted.PubMed.

Awards:

1) Recipient of the National Institutes of Health Chemistry/Biology Interface Training Grant from July 2005 - July 2007.
2) Recipient of the “Graduate Student Conference Grant” on behalf of the American Crystallographic Association in recognition of academic excellence as a student (2006 and 2007)
3) Recipient of the Cornell Conference Travel Award 2006 and 2007
4) Recipient of a Pauling Prize for a best student poster presentation; American Crystallographic Association Annual Meeting, Salt Lake City, UT; July 25, 2007.

Structure

Structure of purine nucleoside phosphorylase from Thermotoga maritima rendered in PyMOL. PDB code: 1VMK

Purine nucleoside phosphorylase (PNP) enzymes are involved in the purine salvage pathway through reversible catalysis of purine nucleosides to generate a purine base and ribose 1-phosphate. This salvage pathway allows for the cell to metabolize preformed nucleotides into precursors for the synthesis of other nucleotides, thus bypassing the need for de novo nucleotide biosynthesis.