Brookhaven National Laboratory The Rockefeller University and  Albert Einstein College of Medicine

Proteins from yeast are chosen to represent evolutionarily diverse families whose members are not predicted to correspond to a known protein structure (based on Sali Lab Yeast Protein Models ). The initial protein families were selected from clusters generated on the basis of sequence similarity by SYSTERS, PRODOM, and DOMO. Coding sequences obtained by PCR from genomic DNA are cloned, expressed, purified and crystallized for structure determination. Information about the proteins is provided and progress toward determination of the structures is summarized in the data tables. Proteins P013-P016 were chosen to test whether the structure prediction tools did in fact discover structural similarity between proteins that align with only 14-22% identity in amino-acid sequence.
 

The primary objective is to put in place the technology needed to increase knowledge of the diversity of protein folds in nature. This basic information is needed to develop computational tools for predicting protein structures from gene sequences and for predicting protein function from structure. These tools will ultimately be applied to understand the functions and interactions of the 100,000 or so proteins of the human proteome.

Collaborators:

 

Brookhaven National Laboratory	Bill Studier, Joel Sussman, S. Swaminathan, Otto Ritter Dawei Lin, Jiansheng Jiang, S. Eswaramoorthy  Bob Sweet, Malcolm Capel, Hal Lewis, John Flanagan Sue Ellen Gerchman, Helen Kycia, Vito Graziano, Nancy Manning
The Rockefeller University	Stephen Burley, Andrej Sali, Terry Gaasterland Jeff Bonanno, Roberto Sanchez, Natalia Rodionova
Albert Einstein College of Medicine	Mark Chance, Steve Almo

Support:

This Pilot Project is part of the Joint Genome Institute (JGI) Functional Genomics Program, supported by the Office of Biological and Environmental Research (OBER) of the U.S. Department of Energy.

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