1M1P

P21 crystal structure of the tetraheme cytochrome c3 from Shewanella oneidensis MR1

1M1P の概要

• エントリーDOI: 10.2210/pdb1m1p/pdb
• 関連するPDBエントリー: 1M1Q 1M1R
• 分子名称: Small tetraheme cytochrome c, SULFATE ION, HEME C, ... (4 entities in total)
• 機能のキーワード: tetraheme cytochrome c, electron transport
• 由来する生物種: Shewanella oneidensis
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 73270.05

構造登録者

Leys, D.,Meyer, T.E.,Tsapin, A.I.,Nealson, K.H.,Cusanovich, M.A.,Van Beeumen, J.J. (登録日: 2002-06-20, 公開日: 2002-08-14, 最終更新日: 2024-11-20)

主引用文献

Leys, D.,Meyer, T.E.,Tsapin, A.I.,Nealson, K.H.,Cusanovich, M.A.,Van Beeumen, J.J.
Crystal structures at atomic resolution reveal the novel concept of 'electron-harvesting' as a role for the small tetraheme cytochrome c
J.Biol.Chem., 277:35703-35711, 2002

PubMed Abstract: The genus Shewanella produces a unique small tetraheme cytochrome c that is implicated in the iron oxide respiration pathway. It is similar in heme content and redox potential to the well known cytochromes c(3) but related in structure to the cytochrome c domain of soluble fumarate reductases from Shewanella sp. We report the crystal structure of the small tetraheme cytochrome c from Shewanella oneidensis MR-1 in two crystal forms and two redox states. The overall fold and heme core are surprisingly different from the soluble fumarate reductase structures. The high resolution obtained for an oxidized orthorhombic crystal (0.97 A) revealed several flexible regions. Comparison of the six monomers in the oxidized monoclinic space group (1.55 A) indicates flexibility in the C-terminal region containing heme IV. The reduced orthorhombic crystal structure (1.02 A) revealed subtle differences in the position of several residues, resulting in decreased solvent accessibility of hemes and the withdrawal of a positive charge from the molecular surface. The packing between monomers indicates that intermolecular electron transfer between any heme pair is possible. This suggests there is no unique site of electron transfer on the surface of the protein and that electron transfer partners may interact with any of the hemes, a process termed "electron-harvesting." This optimizes the efficiency of intermolecular electron transfer by maximizing chances of productive collision with redox partners.

PubMed: 12080059
DOI: 10.1074/jbc.M203866200

実験手法

X-RAY DIFFRACTION (1.55 Å)