1ycd: Difference between revisions

Revision as of 17:04, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ycd.png

Template:STRUCTURE 1ycd

Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase familyCrystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family

Template:ABSTRACT PUBMED 15802654

About this StructureAbout this Structure

1YCD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family., Quevillon-Cheruel S, Leulliot N, Graille M, Hervouet N, Coste F, Benedetti H, Zelwer C, Janin J, Van Tilbeurgh H, Protein Sci. 2005 May;14(5):1350-6. Epub 2005 Mar 31. PMID:15802654

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family'''
+===Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family===
-==Overview==
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-Yhr049w/FSH1 was recently identified in a combined computational and experimental proteomics analysis for the detection of active serine hydrolases in yeast. This analysis suggested that FSH1 might be a serine-type hydrolase belonging to the broad functional alphabeta-hydrolase superfamily. In order to get insight into the molecular function of this gene, it was targeted in our yeast structural genomics project. The crystal structure of the protein confirms that it contains a Ser/His/Asp catalytic triad that is part of a minimal alpha/beta-hydrolase fold. The architecture of the putative active site and analogies with other protein structures suggest that FSH1 may be an esterase. This finding was further strengthened by the unexpected presence of a compound covalently bound to the catalytic serine in the active site. Apparently, the enzyme was trapped with a reactive compound during the purification process.
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