1BQ3

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE

1BQ3 の概要

• エントリーDOI: 10.2210/pdb1bq3/pdb
• 分子名称: PROTEIN (PHOSPHOGLYCERATE MUTASE 1), INOSITOL HEXAKISPHOSPHATE, SULFATE ION (3 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: 4
• 化学式量合計: 111773.80

構造登録者

Rigden, D.J.,Phillips, S.E.V.,Fothergill-Gilmore, L.A. (登録日: 1998-08-20, 公開日: 1998-08-26, 最終更新日: 2023-08-09)

主引用文献

Rigden, D.J.,Walter, R.A.,Phillips, S.E.,Fothergill-Gilmore, L.A.
Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis.
J.Mol.Biol., 289:691-699, 1999

PubMed Abstract: The effects that the inhibitors inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates have on the phosphoglycerate mutases from Saccharomyces cerevisiae and Schizosaccharomyces pombe have been determined. Their Kivalues have been calculated, and the ability of the inhibitors to protect the enzymes against limited proteolysis investigated. These biochemical data have been placed in a structural context by the solution of the crystal structures of S. cerevisiae phosphoglycerate mutase soaked with inositol hexakisphosphate or benzene hexacarboxylate. These large polyanionic compounds bind to the enzyme so as to block the entrance to the active-site cleft. They form multiple interactions with the enzyme, consistent with their low Kivalues, and afford good protection against limited proteolysis of the C-terminal region by thermolysin. The inositol compound is more efficacious because of its greater number of negative charges. The S. pombe phosphoglycerate mutase that is inherently lacking a comparable C-terminal region has higher Kivalues for the compounds tested. Moreover, the S. pombe enzyme is less sensititive to proteolysis, and the presence or absence of the inhibitor molecules has little effect on susceptibility to proteolysis.

PubMed: 10369755
DOI: 10.1006/jmbi.1999.2848

実験手法

X-RAY DIFFRACTION (2.7 Å)