2WFP

Crystal structure of mannose 6-phosphate isomerase (apo form) from Salmonella typhimurium

2WFP の概要

• エントリーDOI: 10.2210/pdb2wfp/pdb
• 分子名称: MANNOSE-6-PHOSPHATE ISOMERASE, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: isomerase, apo-structure, metal-binding
• 由来する生物種: SALMONELLA TYPHIMURIUM
• 細胞内の位置: Cytoplasm (Probable): P25081
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43914.97

構造登録者

Sagurthi, S.R. (登録日: 2009-04-13, 公開日: 2009-07-14, 最終更新日: 2024-05-08)

主引用文献

Sagurthi, S.R.,Gowda, G.,Savithri, H.S.,Murthy, M.R.N.
Crystal Structures of Mannose 6-Phosphate Isomerase from Salmonella Typhimurium Bound to Metal Atoms and Substrate: Implications for Catalytic Mechanism
Acta Crystallogr.,Sect.D, 65:724-, 2009

PubMed Abstract: Mannose-6-phosphate isomerase (MPI) catalyzes the interconversion of mannose 6-phosphate and fructose 6-phosphate. X-ray crystal structures of MPI from Salmonella typhimurium in the apo form (with no metal bound) and in the holo form (with bound Zn2+) and two other structures with yttrium bound at an inhibitory site and complexed with Zn2+ and fructose 6-phosphate (F6P) were determined in order to gain insights into the structure and the isomerization mechanism. Isomerization involves acid/base catalysis with proton transfer between the C1 and C2 atoms of the substrate. His99, Lys132, His131 and Asp270 are close to the substrate and are likely to be the residues involved in proton transfer. The interactions observed at the active site suggest that the ring-opening step is probably catalyzed by His99 and Asp270. An active-site loop consisting of residues 130-133 undergoes conformational changes upon substrate binding. Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site. Isomerization probably follows the previously suggested cis-enediol mechanism.

PubMed: 19564693
DOI: 10.1107/S0907444909013328

実験手法

X-RAY DIFFRACTION (1.67 Å)