1la2
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(New page: 200px<br /><applet load="1la2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1la2, resolution 2.65Å" /> '''Structural analysis ...)
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Revision as of 18:17, 20 November 2007
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Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase
Overview
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.
About this Structure
1LA2 is a Single protein structure of sequence from Saccharomyces cerevisiae with NAD as ligand. Active as Inositol-3-phosphate synthase, with EC number 5.5.1.4 Full crystallographic information is available from OCA.
Reference
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase., Kniewel R, Buglino JA, Shen V, Chadha T, Beckwith A, Lima CD, J Struct Funct Genomics. 2002;2(3):129-34. PMID:12836703
Page seeded by OCA on Tue Nov 20 20:25:10 2007
Categories: Inositol-3-phosphate synthase | Saccharomyces cerevisiae | Single protein | Beckwith, A. | Buglino, J.A. | Burley, S.K. | Chadna, T. | Kniewel, R. | Lima, C.D. | NYSGXRC, New.York.Structural.GenomiX.Research.Consortium. | Shen, V. | NAD | Ino1 | Inositol | Metabolism | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics | Yeast
