1LA2

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase

1LA2 の概要

• エントリーDOI: 10.2210/pdb1la2/pdb
• 分子名称: Myo-inositol-1-phosphate synthase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: structural genomics, inositol, metabolism, yeast, ino1, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, isomerase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 243360.54

構造登録者

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) (登録日: 2002-03-27, 公開日: 2002-04-10, 最終更新日: 2024-11-06)

主引用文献

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

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: 12836703
DOI: 10.1023/A:1021293408654

実験手法

X-RAY DIFFRACTION (2.65 Å)