2agk: Difference between revisions

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[[Image:2agk.gif|left|200px]]
{{Seed}}
[[Image:2agk.png|left|200px]]


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{{STRUCTURE_2agk|  PDB=2agk  |  SCENE=  }}  
{{STRUCTURE_2agk|  PDB=2agk  |  SCENE=  }}  


'''Structure of S. cerevisiae His6 protein'''
===Structure of S. cerevisiae His6 protein===




==Overview==
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The Saccharomyces cerevisiae His6 gene codes for the enzyme phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase, catalyzing the fourth step in histidine biosynthesis. To get an insight into the structure and function of this enzyme, we determined its X-ray structure at a resolution of 1.30 A using the anomalous diffraction signal of the protein's sulphur atoms at 1.77 A wavelength. His6 folds in an (alpha/beta)8 barrel similar to HisA, which performs the same function in bacteria and archaea. We found a citrate molecule from the buffer bound in a pocket near the expected position of the active site and used it to model the open form of the substrate (phosphoribulosyl moiety), which is a reaction intermediate. This model enables us to identify catalytic residues and to propose a reaction mechanism where two aspartates act as acid/base catalysts: Asp134 as a proton donor for ring opening, and Asp9 as a proton acceptor and donor during enolization of the aminoaldose. Asp9 is conserved in yeast His6 and bacterial or archaeal HisA sequences, and Asp134 has equivalents in both HisA and TrpF, but they occur at a different position in the protein sequence.
The line below this paragraph, {{ABSTRACT_PUBMED_16731983}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16731983 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16731983}}


==About this Structure==
==About this Structure==
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[[Category: Tim alpha/beta barrel]]
[[Category: Tim alpha/beta barrel]]
[[Category: Ysg]]
[[Category: Ysg]]
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Revision as of 03:13, 29 July 2008

File:2agk.png

Template:STRUCTURE 2agk

Structure of S. cerevisiae His6 protein

Template:ABSTRACT PUBMED 16731983

About this Structure

2AGK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the yeast His6 enzyme suggests a reaction mechanism., Quevillon-Cheruel S, Leulliot N, Graille M, Blondeau K, Janin J, van Tilbeurgh H, Protein Sci. 2006 Jun;15(6):1516-21. PMID:16731983

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