1DW0

STRUCTURE OF OXIDIZED SHP, AN OXYGEN BINDING CYTOCHROME C

1DW0 の概要

• エントリーDOI: 10.2210/pdb1dw0/pdb
• 関連するPDBエントリー: 1DW1 1DW2 1DW3
• 分子名称: CYTOCHROME C, SULFATE ION, HEME C, ... (4 entities in total)
• 機能のキーワード: cytochrome c, asparagine ligation, oxygen binding, disulfide bridge, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Rhodobacter sphaeroides
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 36757.01

構造登録者

Leys, D.,Backers, K.,Meyer, T.E.,Hagen, W.R.,Cusanovich, M.A.,Van Beeumen, J.J. (登録日: 2000-01-24, 公開日: 2000-06-28, 最終更新日: 2024-10-30)

主引用文献

Leys, D.,Backers, K.,Meyer, T.E.,Hagen, W.R.,Cusanovich, M.A.,Van Beeumen, J.J.
Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides.
J.Biol.Chem., 275:16050-16056, 2000

PubMed Abstract: The photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP), which is an unusual c-type cytochrome capable of transiently binding oxygen during autooxidation. Similar proteins have not only been observed in other photosynthetic bacteria but also in the obligate methylotroph Methylophilus methylotrophus and the metal reducing bacterium Shewanella putrefaciens. A three-dimensional structure of SHP was derived using the multiple isomorphous replacement phasing method. Besides a model for the oxidized state (to 1.82 A resolution), models for the reduced state (2.1 A resolution), the oxidized molecule liganded with cyanide (1. 90 A resolution), and the reduced molecule liganded with nitric oxide (2.20 A resolution) could be derived. The SHP structure represents a new variation of the class I cytochrome c fold. The oxidized state reveals a novel sixth heme ligand, Asn(88), which moves away from the iron upon reduction or when small molecules bind. The distal side of the heme has a striking resemblance to other heme proteins that bind gaseous compounds. In SHP the liberated amide group of Asn(88) stabilizes solvent-shielded ligands through a hydrogen bond.

PubMed: 10821858
DOI: 10.1074/jbc.275.21.16050

実験手法

X-RAY DIFFRACTION (1.82 Å)