1CCJ

CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY

1CCJ の概要

• エントリーDOI: 10.2210/pdb1ccj/pdb
• 分子名称: CYTOCHROME C PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: oxidoreductase, peroxidase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion matrix: P00431
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34113.78

構造登録者

Cao, Y.,Musah, R.A.,Wilcox, S.K.,Goodin, D.B.,Mcree, D.E. (登録日: 1997-01-22, 公開日: 1997-07-23, 最終更新日: 2024-05-22)

主引用文献

Cao, Y.,Musah, R.A.,Wilcox, S.K.,Goodin, D.B.,McRee, D.E.
Protein conformer selection by ligand binding observed with crystallography.
Protein Sci., 7:72-78, 1998

PubMed Abstract: A large-scale movement between "closed" and "open" conformations of a protein loop was observed directly with protein crystallography by trapping individual conformers through binding of an exogenous ligand and characterization with solution kinetics. The buried indole ring of Trp191 in cytochrome c peroxidase (CCP) was displaced by exogenous ligands, causing a conformational change of loop Pro190-Asn195 and exposing Trp191 to the protein surface. Kinetic measurements are consistent with a two-step binding mechanism in which the rate-limiting step is a transition of the protein to the open state, which then binds the ligand. This large-scale conformational change of a functionally important region of CCP is independent of ligand and indicates that about 4% of the wild-type protein is in the open form in solution at any given time.

PubMed: 9514261

実験手法

X-RAY DIFFRACTION (2.1 Å)