5E78

Crystal structure of P450 BM3 heme domain variant complexed with Co(III)Sep

5E78 の概要

• エントリーDOI: 10.2210/pdb5e78/pdb
• 分子名称: Bifunctional P-450/NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, COBALT (II) ION, ... (6 entities in total)
• 機能のキーワード: bm3, p450, mediated electron transport, co(iii)sep, oxidoreductase
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105628.12

構造登録者

Panneerselvm, S.,Shehzad, A.,Bocola, M.,Mueller-Dieckmann, J.,Schwaneberg, U. (登録日: 2015-10-12, 公開日: 2016-09-28, 最終更新日: 2024-01-10)

主引用文献

Panneerselvam, S.,Shehzad, A.,Mueller-Dieckmann, J.,Wilmanns, M.,Bocola, M.,Davari, M.D.,Schwaneberg, U.
Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.
Biochim. Biophys. Acta, 1866:134-140, 2018

PubMed Abstract: P450 BM3 is a multi-domain heme-containing soluble bacterial monooxygenase. P450 BM3 and variants are known to oxidize structurally diverse substrates. Crystal structures of individual domains of P450 BM3 are available. However, the spatial organization of the full-length protein is unknown. In this study, crystal structures of the P450 BM3 M7 heme domain variant with and without cobalt (III) sepulchrate are reported. Cobalt (III) sepulchrate acts as an electron shuttle in an alternative cofactor system employing zinc dust as the electron source. The crystal structure shows a binding site for the mediator cobalt (III) sepulchrate at the entrance of the substrate access channel. The mediator occupies an unusual position which is far from the active site and distinct from the binding of the natural redox partner (FAD/NADPH binding domain).

PubMed: 28739446
DOI: 10.1016/j.bbapap.2017.07.010

実験手法

X-RAY DIFFRACTION (2 Å)