Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics.

Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Research Abstract Details 

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Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Abstract Text:

Rakhi Agarwal,Stephen K Burley,Subramanyam Swaminathan,

Purine metabolism plays a major role in regulating the availability of purine nucleotides destined for nucleic acid synthesis. Allantoate amidohydrolase catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. The crystal structure of a ternary complex of allantoate amidohydrolase with its substrate allantoate and an allosteric effector, a sulfate ion, from Escherichia coli was determined to understand better the catalytic mechanism and substrate specificity. The 2.25 A resolution X-ray structure reveals an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family and lacks the (beta/alpha)(8)-barrel fold characteristic of the amidohydrolases. Arrangement of the substrate and the two co-catalytic zinc ions at the active site governs catalytic specificity for hydrolysis of N-carbamyl versus the peptide bond in exopeptidases. In its crystalline form, allantoate amidohydrolase adopts a relatively open conformation. However, structural analysis reveals the possibility of a significant movement of domains via rotation about two hinge regions upon allosteric effector and substrate binding resulting in a closed catalytically competent conformation by bringing the substrate allantoate closer to co-catalytic zinc ions. Two cis-prolyl peptide bonds found on either side of the dimerization domain in close proximity to the substrate and ligand-binding sites may be involved in protein folding and in preserving the integrity of the catalytic site.

Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Publishing Authors By Initials

R Agarwal,SK Burley,S Swaminathan,

For similar inorganic chemicals: elements: metals, heavy: zinc research abstracts see: inorganic chemicals: elements: metals, heavy: zinc research

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Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of molecular biology

VOLUME: 368

Page Numbers: 450-63

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 20

MONTH: 02

YEAR: 2007

Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Keywords Mesh Terms:

KEYWORDS: Zinc

MESH TERMS: metabolism

Chemical & Substance for Abstract: Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. Information

Substance Name: allantoate amidohydrolase

Registry Number: EC 3.5.3.-

Grant and Affiliation Information for Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics.

AFFILIATION: Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM62529

ACRONYM: GM

MEDLINETA: J Mol Biol

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