Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6WPL

Structure of Cytochrome P450tcu

6WPL の概要
エントリーDOI10.2210/pdb6wpl/pdb
分子名称Cytochrome P-450cam, subunit of camphor 5-monooxygenase system, PROTOPORPHYRIN IX CONTAINING FE, 5-EXO-HYDROXYCAMPHOR, ... (5 entities in total)
機能のキーワードcamphor monooxygenase, cytochrome p450, oxidoreductase
由来する生物種Pseudomonas sp. TCU-HL1
タンパク質・核酸の鎖数1
化学式量合計47134.92
構造登録者
Murarka, V.C.,Batabyal, D.,Amaya, J.A.,Sevrioukova, I.F.,Poulos, T.L. (登録日: 2020-04-27, 公開日: 2020-07-01, 最終更新日: 2023-10-18)
主引用文献Murarka, V.C.,Batabyal, D.,Amaya, J.A.,Sevrioukova, I.F.,Poulos, T.L.
Unexpected Differences between Two Closely Related Bacterial P450 Camphor Monooxygenases.
Biochemistry, 59:2743-2750, 2020
Cited by
PubMed Abstract: The bacterial cytochrome P450cam catalyzes the oxidation of camphor to 5--hydroxycamphor as the first step in the oxidative assimilation of camphor as a carbon/energy source. CYP101D1 is another bacterial P450 that catalyzes the same reaction. A third P450 (P450tcu) has recently been discovered that has ≈86% sequence identity to P450cam as well as very similar enzymatic properties. P450tcu, however, exhibits three unusual features not found in P450cam. First, we observe product in at least two orientations in the X-ray structure that indicates that, unlike the case for P450cam, X-ray-generated reducing equivalents can drive substrate hydroxylation . We postulate, on the basis of molecular dynamics simulations, that greater flexibility in P450tcu enables easier access of protons to the active site and, together with X-ray driven reduction, results in O activation and substrate hydroxylation. Second, the characteristic low-spin to high-spin transition when camphor binds occurs immediately with P450cam but is very slow in P450tcu. Third, isothermal titration calorimetry shows that in P450cam substrate binding is entropically driven with a Δ of >0 while in P450tcu with a Δ of <0 with a more modest change in -Δ. These results indicate that despite nearly identical structures and enzymatic properties, these two P450s exhibit quite different properties most likely related to differences in conformational dynamics.
PubMed: 32551522
DOI: 10.1021/acs.biochem.0c00366
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.097 Å)
構造検証レポート
Validation report summary of 6wpl
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

PDB statisticsPDBj update infoContact PDBjnumon