1la2
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase
OverviewOverview
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 StructureAbout this Structure
1LA2 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 23:42:51 2008
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OCA- Pages with broken file links
- 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.
- Ino1
- Inositol
- Metabolism
- New york structural genomix research consortium
- Nysgxrc
- Protein structure initiative
- Psi
- Structural genomic
- Yeast