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Combining High‐Throughput Structure Determination and Enzyme Characterization for Functional Annotation of a Large Enzyme Superfamily
Author(s) -
Burley Stephen Kevin
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb233
Subject(s) - structural genomics , computational biology , amidohydrolase , enzyme , functional genomics , function (biology) , superfamily , biology , genomics , protein structure , biochemistry , genetics , genome , gene
Under the auspices of the NIH Protein Structure Initiative (PSI), the New York SGX Research Center for Structural Genomics (NYSGXRC) developed a high‐throughput X‐ray crystallography platform that currently produces more than 200 de novo protein structures annually at an average cost of ~$40,000 per structure. As required by the PSI, ~15% of NYSGXRC efforts have been devoted to studies of targets nominated by members of the scientific community. The majority of our Community Targets were pursued in collaboration with an NIH‐funded P01 Program Project, entitled “Deciphering Enzyme Specificity” (GM071790; Principal Investigator: John Gerlt). Together, the P01 and the NYSGXRC examined the large Enolase/Amidohydrolase enzyme superfamily, with the goal of establishing a scalable experimental/bioinformatic platform for large‐scale functional characterization that supports prediction of enzyme function from sequence or structure. To date, the NYSGXRC has determined experimental structures of more than 70 Enolases and 30 Amidohydrolases plus more than 20 operon/pathway‐related enzymes. Illustrative successes from this synergistic systems structural genomics collaboration will be presented.