2LQT

Solution structure of CHCHD7

2LQT の概要

• エントリーDOI: 10.2210/pdb2lqt/pdb
• 関連するPDBエントリー: 2LQL
• NMR情報: BMRB: 18328
• 分子名称: Coiled-coil-helix-coiled-coil-helix domain-containing protein 7 (1 entity in total)
• 機能のキーワード: chch domain, mitochondrial import, alpha-hairpin, mia40-dependent disulfide relay system, unknown function
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10110.51

構造登録者

Winkelmann, J.,Ciofi-Baffoni, S.,Banci, L.,Bertini, I. (登録日: 2012-03-14, 公開日: 2012-10-24, 最終更新日: 2024-10-30)

主引用文献

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Jaiswal, D.,Neri, S.,Peruzzini, R.,Winkelmann, J.
Structural characterization of CHCHD5 and CHCHD7: Two atypical human twin CX(9)C proteins.
J.Struct.Biol., 180:190-200, 2012

PubMed Abstract: Twin CX(9)C proteins constitute a large protein family among all eukaryotes; are putative substrates of the mitochondrial Mia40-dependent import machinery; contain a coiled coil-helix-coiled coil-helix (CHCH) fold stabilized by two disulfide bonds as exemplified by three structures available for this family. However, they considerably differ at the primary sequence level and this prevents an accurate prediction of their structural models. With the aim of expanding structural information on CHCH proteins, here we structurally characterized human CHCHD5 and CHCHD7. While CHCHD5 has two weakly interacting CHCH domains which sample a range of limited conformations as a consequence of hydrophobic interactions, CHCHD7 has a third helix hydrophobically interacting with an extension of helix α2, which is part of the CHCH domain. Upon reduction of the disulfide bonds both proteins become unstructured exposing hydrophobic patches, with the result of protein aggregation/precipitation. These results suggest a model where the molecular interactions guiding the protein recognition between Mia40 and the disulfide-reduced CHCHD5 and CHCHD7 substrates occurs in vivo when the latter proteins are partially embedded in the protein import pore of the outer membrane of mitochondria.

PubMed: 22842048
DOI: 10.1016/j.jsb.2012.07.007

実験手法

SOLUTION NMR