1la2 | pdb_00001la2

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase

File:1la2.gif

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1la2, resolution 2.65Å
Ligands:	MSE, NAD
Gene:	INO1 (Saccharomyces cerevisiae)
Activity:	Inositol-3-phosphate synthase, with EC number 5.5.1.4
Domains:	INO1, NAD_binding_5
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

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. 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

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