Literature DB >> 12836703

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.

Ryan Kniewel1, John A Buglino, Vincent Shen, Tanya Chadha, Andrew Beckwith, Christopher D Lima.   

Abstract

The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.

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Year:  2002        PMID： 12836703     DOI： 10.1023/a:1021293408654

Source DB:  PubMed          Journal:  J Struct Funct Genomics        ISSN： 1345-711X


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  3 in total

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Authors:  Kelly Neelon; Mary F Roberts; Boguslaw Stec
Journal:  Biophys J       Date:  2011-12-07       Impact factor: 4.033

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Authors:  Rania M Deranieh; Quan He; Joseph A Caruso; Miriam L Greenberg
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  3 in total

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