NDLI: Crystal structure of the yeast His6 enzyme suggests a reaction mechanism.

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Crystal structure of the yeast His6 enzyme suggests a reaction mechanism.

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Crystal structure of the yeast His6 enzyme suggests a reaction mechanism.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Blondeau, Karine Graille, Marc Leulliot, Nicolas Van Tilbeurgh, Herman Quevillon-Cheruel, Sophie Janin, Joel
Description	Country affiliation: France Author Affiliation: Quevillon-Cheruel S ( Institut de Biochimie et de Biophysique Moléculaire et Cellulaire (CNRS-UMR 8619), Université Paris-Sud, 91405 Orsay, France.)
Abstract	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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	15
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2006-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aldose-ketose Isomerases Chemistry Metabolism Saccharomyces Cerevisiae Proteins Aminohydrolases Aspartic Acid Binding Sites Catalytic Domain Citrates Crystallography, X-ray Models, Molecular Protein Conformation Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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