5PGM

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

5PGM の概要

• エントリーDOI: 10.2210/pdb5pgm/pdb
• 分子名称: PHOSPHOGLYCERATE MUTASE 1, SULFATE ION, ALANINE, ... (4 entities in total)
• 機能のキーワード: isomerase, transferase (phosphoryl), glycolytic enzyme
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 221765.05

構造登録者

Rigden, D.J.,Phillips, S.E.V.,Fothergill-Gilmore, L.A. (登録日: 1998-08-19, 公開日: 1999-02-16, 最終更新日: 2024-12-25)

主引用文献

Rigden, D.J.,Walter, R.A.,Phillips, S.E.,Fothergill-Gilmore, L.A.
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.
J.Mol.Biol., 286:1507-1517, 1999

PubMed Abstract: The structure of a new crystal form of Saccharomyces cerevisiae phosphoglycerate mutase has been solved and refined to 2.12 A with working and free R-factors of 19.7 and 22.9 %, respectively. Higher-resolution data and greater non-crystallographic symmetry have produced a more accurate protein structure than previously. Prominent among the differences from the previous structure is the presence of two sulphate ions within each active site cleft. The separation of the sulphates suggests that they may occupy the same sites as phospho groups of the bisphosphate ligands of the enzyme. Plausible binding modes for 2,3-bisphosphoglycerate and 1, 3-bisphosphoglycerate are thereby suggested. These results support previous conclusions from mutant studies, highlight interesting new targets for mutagenesis and suggest a possible mechanism of enzyme phosphorylation.

PubMed: 10064712
DOI: 10.1006/jmbi.1999.2566

実験手法

X-RAY DIFFRACTION (2.12 Å)