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PDBsum entry 1la2

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
1la2
Jmol
Contents
Protein chains
514 a.a. *
Ligands
NAD ×4
Waters ×692
* Residue conservation analysis
PDB id:
1la2
Name: Isomerase
Title: Structural analysis of saccharomyces cerevisiae myo- inositol phosphate synthase
Structure: Myo-inositol-1-phosphate synthase. Chain: a, b, c, d. Synonym: mi-1-p synthase, ips. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: ino1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
2.65Å     R-factor:   0.224     R-free:   0.280
Authors: R.Kniewel,J.A.Buglino,V.Shen,T.Chadna,A.Beckwith,C.D.Lima, S.K.Burley,New York Sgx Research Center For Structural Genomics (Nysgxrc)
Key ref: R.Kniewel et al. (2002). Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase. J Struct Funct Genomics, 2, 129-134. PubMed id: 12836703
Date:
27-Mar-02     Release date:   10-Apr-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P11986  (INO1_YEAST) -  Inositol-3-phosphate synthase
Seq:
Struc:
 
Seq:
Struc:
533 a.a.
514 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.5.1.4  - Inositol-3-phosphate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
myo-Inositol Biosynthesis
      Reaction: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
D-glucose 6-phosphate
= 1D-myo-inositol 3-phosphate
      Cofactor: NAD(+)
NAD(+)
Bound ligand (Het Group name = NAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     lipid metabolic process   3 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
    reference    
 
 
J Struct Funct Genomics 2:129-134 (2002)
PubMed id: 12836703  
 
 
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.
R.Kniewel, J.A.Buglino, V.Shen, T.Chadha, A.Beckwith, C.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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17390001 P.M.Flatt, and T.Mahmud (2007).
Biosynthesis of aminocyclitol-aminoglycoside antibiotics and related compounds.
  Nat Prod Rep, 24, 358-392.  
15016817 M.Majee, S.Maitra, K.G.Dastidar, S.Pattnaik, A.Chatterjee, N.C.Hait, K.P.Das, and A.L.Majumder (2004).
A novel salt-tolerant L-myo-inositol-1-phosphate synthase from Porteresia coarctata (Roxb.) Tateoka, a halophytic wild rice: molecular cloning, bacterial overexpression, characterization, and functional introgression into tobacco-conferring salt tolerance phenotype.
  J Biol Chem, 279, 28539-28552.  
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