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1b54
From Proteopedia
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'''CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT''' | '''CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT''' | ||
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | ||
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
| - | [[Category: | + | [[Category: New york structural genomix research consortium]] |
| - | [[Category: | + | [[Category: Nysgxrc]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Proteome]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Pyridoxal phosphate]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Tim barrel]] |
| - | [[Category: | + | [[Category: Yeast hypothetical protein]] |
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Revision as of 08:04, 2 May 2008
CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT
Overview
Yeast hypothetical protein YBL036C (SWISS-PROT P38197), initially thought to be a member of an 11-protein family, was selected for crystal structure determination since no structural or functional information was available. The structure has been determined independently by MIR and MAD methods to 2.0 A resolution. The MAD structure was determined largely through automated model building. The protein folds as a TIM barrel beginning with a long N-terminal helix, in contrast to the classic triose phosphate isomerase (TIM) structure, which begins with a beta-strand. A cofactor, pyridoxal 5'-phosphate, is covalently bound near the C-terminal end of the barrel, the usual active site in TIM-barrel folds. A single-domain monomeric molecule, this yeast protein resembles the N-terminal domain of alanine racemase or ornithine decarboxylase, both of which are two-domain dimeric proteins. The yeast protein has been shown to have amino-acid racemase activity. Although selected as a member of a protein family having no obvious relationship to proteins of known structure, the protein fold turned out to be a well known and widely distributed fold. This points to the need for a more comprehensive base of structural information and better structure-modeling tools before the goal of structure prediction from amino-acid sequences can be realised. In this case, similarity to a known structure allowed inferences to be made about the structure and function of a widely distributed protein family.
About this Structure
1B54 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of a yeast hypothetical protein selected by a structural genomics approach., Eswaramoorthy S, Gerchman S, Graziano V, Kycia H, Studier FW, Swaminathan S, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):127-35. Epub 2002, Dec 19. PMID:12499548 Page seeded by OCA on Fri May 2 11:04:57 2008
Categories: Saccharomyces cerevisiae | Single protein | Burley, S K. | Eswaramoorthy, S. | NYSGXRC, New York Structural GenomiX Research Consortium. | Swaminathan, S. | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Proteome | Psi | Pyridoxal phosphate | Structural genomic | Tim barrel | Yeast hypothetical protein
