2QBO

Crystal structure of the P450cam G248V mutant in the cyanide bound state

2QBO の概要

• エントリーDOI: 10.2210/pdb2qbo/pdb
• 関連するPDBエントリー: 2QBL 2QBM 2QBN
• 分子名称: Cytochrome P450-cam, CYANIDE ION, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: cyp101, mutant, conserved active site residue, cyanide complex, gly248, heme geometry, oxidoreductase
• 由来する生物種: Pseudomonas putida
• 細胞内の位置: Cytoplasm : P00183
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48424.86

構造登録者

von Koenig, K.,Makris, T.M.,Sligar, S.D.,Schlichting, I. (登録日: 2007-06-18, 公開日: 2007-12-25, 最終更新日: 2023-08-30)

主引用文献

Makris, T.M.,Koenig, K.V.,Schlichting, I.,Sligar, S.G.
Alteration of P450 Distal Pocket Solvent Leads to Impaired Proton Delivery and Changes in Heme Geometry.
Biochemistry, 46:14129-14140, 2007

PubMed Abstract: Distal pocket water molecules have been widely implicated in the delivery of protons required in O-O bond heterolysis in the P450 reaction cycle. Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket through mutagenesis of a distal pocket glycine to either valine or threonine results in the alteration of spin state equilibria, and has dramatic consequences on the catalytic rate, coupling efficiency, and kinetic solvent isotope effect parameters, highlighting an important role of the active-site hydration level on P450 catalysis. Cryoradiolysis of the mutant CYP101 oxyferrous complexes further indicates a specific perturbation of proton-transfer events required for the transformation of ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of the 248Val and 248Thr mutants in both the ferric camphor bound resting state and ferric-cyano adducts shows both the alteration of hydrogen-bonding networks and the alteration of heme geometry parameters. Taken together, these results indicate that the distal pocket microenvironment governs the transformation of reactive heme-oxygen intermediates in P450 cytochromes.

PubMed: 18001135
DOI: 10.1021/bi7013695

実験手法

X-RAY DIFFRACTION (1.9 Å)