4EIC

Crystal structure of reduced cytochrome c6 from Synechococcus sp. PCC 7002 at ultra-high resolution

4EIC の概要

• エントリーDOI: 10.2210/pdb4eic/pdb
• 関連するPDBエントリー: 3DR0 4EID 4EIE 4EIF
• 分子名称: Cytochrome c6, HEME C, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: electron transport, cytochrome c6
• 由来する生物種: Synechococcus sp.
• 細胞内の位置: Cellular thylakoid lumen (Potential): O30881
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10260.17

構造登録者

Krzywda, S.,Bialek, W.,Jaskolski, M.,Szczepaniak, A. (登録日: 2012-04-05, 公開日: 2013-04-10, 最終更新日: 2025-11-12)

主引用文献

Bialek, W.,Krzywda, S.,Zatwarnicki, P.,Jaskolski, M.,Kolesinski, P.,Szczepaniak, A.
Insights into the relationship between the haem-binding pocket and the redox potential of c6 cytochromes: four atomic resolution structures of c6 and c6-like proteins from Synechococcus sp. PCC 7002.
Acta Crystallogr.,Sect.D, 70:2823-2832, 2014

PubMed Abstract: The structure of cytochrome c6C from the mesophilic cyanobacterium Synechococcus sp. PCC 7002 has been determined at 1.03 Å resolution. This is the first structural report on the recently discovered cyanobacterial cytochrome c6-like proteins found in marine and nitrogen-fixing cyanobacteria. Despite high similarity in the overall three-dimensional fold between cytochromes c6 and c6C, the latter shows saliently different electrostatic properties in terms of surface charge distribution and dipole moments. Its midpoint redox potential is less than half of the value for typical c6 cytochromes and results mainly from the substitution of one residue in the haem pocket. Here, high-resolution crystal structures of mutants of both cytochromes c6 and c6C are presented, and the impact of the mutation of specific residues in the haem-binding pocket on the redox potential is discussed. These findings contribute to the elucidation of the structure-function relationship of c6-like cytochromes.

PubMed: 25372674
DOI: 10.1107/S1399004714013108

実験手法

X-RAY DIFFRACTION (0.84 Å)