2HPD

CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S

2HPD の概要

• エントリーDOI: 10.2210/pdb2hpd/pdb
• 分子名称: CYTOCHROME P450 BM-3, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: oxidoreductase(oxygenase)
• 由来する生物種: Bacillus megaterium
• 細胞内の位置: Cytoplasm (By similarity): P14779
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108825.56

構造登録者

Ravichandran, K.G.,Boddupalli, S.S.,Hasemann, C.A.,Peterson, J.A.,Deisenhofer, J. (登録日: 1993-09-16, 公開日: 1993-10-31, 最終更新日: 2024-02-14)

主引用文献

Ravichandran, K.G.,Boddupalli, S.S.,Hasermann, C.A.,Peterson, J.A.,Deisenhofer, J.
Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.
Science, 261:731-736, 1993

PubMed Abstract: Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.

PubMed: 8342039

実験手法

X-RAY DIFFRACTION (2 Å)