3A3C

Crystal structure of TIM40/MIA40 fusing MBP, C296S and C298S mutant

3A3C の概要

• エントリーDOI: 10.2210/pdb3a3c/pdb
• 関連するPDBエントリー: 2K3J 2ZXT
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein, LINKER, Mitochondrial intermembrane space import and assembly protein 40, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: mitochondrion, inner membrane space, membrane, disulfide bond transfer, alpha helices, sugar transport, transport, mitochondrion inner membrane, phosphoprotein, protein transport, signal-anchor, transit peptide, translocation, transmembrane
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Mitochondrion inner membrane ; Single- pass type II membrane protein ; Intermembrane side : P36046
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50056.10

構造登録者

Kawano, S.,Naoe, M.,Momose, T.,Watanabe, N.,Endo, T. (登録日: 2009-06-11, 公開日: 2009-08-04, 最終更新日: 2024-10-30)

主引用文献

Kawano, S.,Yamano, K.,Naoe, M.,Momose, T.,Terao, K.,Nishikawa, S.,Watanabe, N.,Endo, T.
Structural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane space.
Proc.Natl.Acad.Sci.USA, 106:14403-14407, 2009

PubMed Abstract: The mitochondrial intermembrane space (IMS) contains many small cysteine-bearing proteins, and their passage across the outer membrane and subsequent folding require recognition and disulfide bond transfer by an oxidative translocator Tim40/Mia40 in the inner membrane facing the IMS. Here we determined the crystal structure of the core domain of yeast Mia40 (Mia40C4) as a fusion protein with maltose-binding protein at a resolution of 3 A. The overall structure of Mia40C4 is a fruit-dish-like shape with a hydrophobic concave region, which accommodates a linker segment of the fusion protein in a helical conformation, likely mimicking a bound substrate. Replacement of the hydrophobic residues in this region resulted in growth defects and impaired assembly of a substrate protein. The Cys296-Cys298 disulfide bond is close to the hydrophobic concave region or possible substrate-binding site, so that it can mediate disulfide bond transfer to substrate proteins. These results are consistent with the growth phenotypes of Mia40 mutant cells containing Ser replacement of the conserved cysteine residues.

PubMed: 19667201
DOI: 10.1073/pnas.0901793106

実験手法

X-RAY DIFFRACTION (2.5 Å)