1LA2
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase
Summary for 1LA2
| Entry DOI | 10.2210/pdb1la2/pdb |
| Descriptor | Myo-inositol-1-phosphate synthase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | structural genomics, inositol, metabolism, yeast, ino1, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, isomerase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 243360.54 |
| Authors | Kniewel, R.,Buglino, J.A.,Shen, V.,Chadna, T.,Beckwith, A.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2002-03-27, release date: 2002-04-10, Last modification date: 2024-11-06) |
| Primary citation | Kniewel, R.,Buglino, J.A.,Shen, V.,Chadna, T.,Beckwith, A.,Lima, C.D. Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase J.STRUCT.FUNCT.GENOM., 2:129-134, 2002 Cited by PubMed 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. PubMed: 12836703DOI: 10.1023/A:1021293408654 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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