1la2

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{{STRUCTURE_1la2| PDB=1la2 | SCENE= }}
{{STRUCTURE_1la2| PDB=1la2 | SCENE= }}
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'''Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase'''
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===Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 12836703 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12836703}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Yeast]]
[[Category: Yeast]]
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Revision as of 09:05, 2 July 2008

Image:1la2.png

Template:STRUCTURE 1la2

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase

Template:ABSTRACT PUBMED 12836703

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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