3CPP

CRYSTAL STRUCTURE OF THE CARBON MONOXY-SUBSTRATE-CYTOCHROME P450-CAM TERNARY COMPLEX

3CPP の概要

• エントリーDOI: 10.2210/pdb3cpp/pdb
• 分子名称: CYTOCHROME P450-CAM, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase(oxygenase)
• 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: 47385.61

構造登録者

Raag, R.,Poulos, T.L. (登録日: 1989-07-05, 公開日: 1990-04-15, 最終更新日: 2024-02-21)

主引用文献

Raag, R.,Poulos, T.L.
Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex.
Biochemistry, 28:7586-7592, 1989

PubMed Abstract: The crystal structure of the ternary complex formed between carbon monoxide (CO), camphor, and ferrous cytochrome P-450CAM has been refined to an R value of 17.9% at 1.9-A resolution. To accommodate the CO molecule, the substrate, camphor, moves about 0.8 A while at the same time remaining in nonbonded contact with CO. The average temperature factor of the camphor atoms is about 50% higher in the CO complex, suggesting that the camphor is more loosely bound in this ternary complex. The Fe-C-O angle is about 166 degrees, and thus, CO appears to be bent from the heme normal, as it is in various CO-globin complexes, due to steric interactions with active site groups. The oxygen atom of the CO molecule is nestled into a groove formed by an unusual helical hydrogen bond in the distal helix between the highly conserved Thr 252 and Gly 248 residues. In the transition from the ferric camphor-bound binary complex to the ferrous CO-camphor-bound ternary complex, the heme iron atom moves into the plane defined by the pyrrole nitrogens by about 0.41 A. Although the axial Cys ligand also moves toward the heme, the S-Fe bond stretches from about 2.20 A in the absence of CO to about 2.41 A once CO has bound.

PubMed: 2611203
DOI: 10.1021/bi00445a013

実験手法

X-RAY DIFFRACTION (1.9 Å)