2MF7

Solution structure of the ims domain of the mitochondrial import protein TIM21 from S. cerevisiae

2MF7 の概要

• エントリーDOI: 10.2210/pdb2mf7/pdb
• 関連するPDBエントリー: 2CIU
• NMR情報: BMRB: 19538
• 分子名称: Mitochondrial import inner membrane translocase subunit TIM21 (1 entity in total)
• 機能のキーワード: membrane, mitochondria, translocation, mitochondrial import protein, ims domain, protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Mitochondrion inner membrane ; Single-pass membrane protein : P53220
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14763.00

構造登録者

Bajaj, R.,Jaremko, L.,Jaremko, M.,Becker, S.,Zweckstetter, M. (登録日: 2013-10-07, 公開日: 2014-10-29, 最終更新日: 2024-05-15)

主引用文献

Bajaj, R.,Jaremko, L.,Jaremko, M.,Becker, S.,Zweckstetter, M.
Molecular Basis of the Dynamic Structure of the TIM23 Complex in the Mitochondrial Intermembrane Space.
Structure, 22:1501-1511, 2014

PubMed Abstract: The presequence translocase TIM23 is a highly dynamic complex in which its subunits can adopt multiple conformations and undergo association-dissociation to facilitate import of proteins into mitochondria. Despite the importance of protein-protein interactions in TIM23, little is known about the molecular details of these processes. Using nuclear magnetic resonance spectroscopy, we characterized the dynamic interaction network of the intermembrane space domains of Tim23, Tim21, Tim50, and Tom22 at single-residue level. We show that Tim23(IMS) contains multiple sites to efficiently interact with the intermembrane space domain of Tim21 and to bind to Tim21, Tim50, and Tom22. In addition, we reveal the atomic details of the dynamic Tim23(IMS)-Tim21(IMS) complex. The combined data support a central role of the intermembrane space domain of Tim23 in the formation and regulation of the presequence translocase.

PubMed: 25263020
DOI: 10.1016/j.str.2014.07.015

実験手法

SOLUTION NMR