2L4D

cytochrome c domain of pp3183 protein from Pseudomonas putida

2L4D の概要

• エントリーDOI: 10.2210/pdb2l4d/pdb
• NMR情報: BMRB: 17236
• 分子名称: SCO1/SenC family protein/cytochrome c, HEME C (2 entities in total)
• 機能のキーワード: cytochrome c, sco, electron transfer, electron transport
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12904.45

構造登録者

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Kozyreva, T.,Mori, M.,Wang, S. (登録日: 2010-10-04, 公開日: 2011-01-26, 最終更新日: 2024-11-06)

主引用文献

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Kozyreva, T.,Mori, M.,Wang, S.
Sco proteins are involved in electron transfer processes
J.Biol.Inorg.Chem., 16:391-403, 2011

PubMed Abstract: Sco proteins are widespread in eukaryotic and in many prokaryotic organisms. They have a thioredoxin-like fold and bind a single copper(I) or copper(II) ion through a CXXXC motif and a conserved His ligand, with both tight and weak affinities. They have been implicated in the assembly of the Cu(A) site of cytochrome c oxidase as copper chaperones and/or thioredoxins. In this work we have structurally characterized a Sco domain which is naturally fused with a typical electron transfer molecule, i.e., cytochrome c, in Pseudomonas putida. The thioredoxin-like Sco domain does not bind copper(II), binds copper(I) with weak affinity without involving the conserved His, and has redox properties consisting of a thioredoxin activity and of the ability of reducing copper(II) to copper(I), and iron(III) to iron(II) of the cytochrome c domain. These findings indicate that the His ligand coordination is the discriminating factor for introducing a metallochaperone function in a thioredoxin-like fold, typically responsible for electron transfer processes. A comparative structural analysis of the Sco domain from P. putida versus eukaryotic Sco proteins revealed structural determinants affecting the formation of a tight-affinity versus a weak-affinity copper binding site in Sco proteins.

PubMed: 21181421
DOI: 10.1007/s00775-010-0735-x

実験手法

SOLUTION NMR