1CI3

CYTOCHROME F FROM THE B6F COMPLEX OF PHORMIDIUM LAMINOSUM

1CI3 の概要

• エントリーDOI: 10.2210/pdb1ci3/pdb
• 分子名称: PROTEIN (CYTOCHROME F), ZINC ION, HEME C, ... (4 entities in total)
• 機能のキーワード: electron transfer protein, complex subunit, electron transport
• 由来する生物種: Phormidium laminosum
• 細胞内の位置: Cellular thylakoid membrane; Single-pass membrane protein (By similarity): P95522
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27211.88

構造登録者

Carrell, C.J.,Schlarb, B.G.,Howe, C.J.,Bendall, D.S.,Cramer, W.A.,Smith, J.L. (登録日: 1999-04-07, 公開日: 1999-08-11, 最終更新日: 2024-11-06)

主引用文献

Carrell, C.J.,Schlarb, B.G.,Bendall, D.S.,Howe, C.J.,Cramer, W.A.,Smith, J.L.
Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum.
Biochemistry, 38:9590-9599, 1999

PubMed Abstract: Cytochrome f from the photosynthetic cytochrome b(6)f complex is unique among c-type cytochromes in its fold and heme ligation. The 1. 9-A crystal structure of the functional, extrinsic portion of cytochrome f from the thermophilic cyanobacterium Phormidium laminosum demonstrates that an unusual buried chain of five water molecules is remarkably conserved throughout the biological range of cytochrome f from cyanobacteria to plants [Martinez et al. (1994) Structure 2, 95-105]. Structure and sequence conservation of the cytochrome f extrinsic portion is concentrated at the heme, in the buried water chain, and in the vicinity of the transmembrane helix anchor. The electrostatic surface potential is variable, so that the surface of P. laminosum cytochrome f is much more acidic than that from turnip. Cytochrome f is unrelated to cytochrome c(1), its functional analogue in the mitochondrial respiratory cytochrome bc(1) complex, although other components of the b(6)f and bc(1) complexes are homologous. Identical function of the two complexes is inferred for events taking place at sites of strong sequence conservation. Conserved sites throughout the entire cytochrome b(6)f/bc(1) family include the cluster-binding domain of the Rieske protein and the heme b and quinone-binding sites on the electrochemically positive side of the membrane within the b cytochrome, but not the putative quinone-binding site on the electrochemically negative side.

PubMed: 10423236
DOI: 10.1021/bi9903190

実験手法

X-RAY DIFFRACTION (1.9 Å)