1HR8

Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C Oxidase IV Signal Peptide

1HR8 の概要

• エントリーDOI: 10.2210/pdb1hr8/pdb
• 関連するPDBエントリー: 1HR6 1HR7 1HR9
• 分子名称: MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT, MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT, CYTOCHROME C OXIDASE POLYPEPTIDE IV, ... (6 entities in total)
• 機能のキーワード: hxxeh zinc-binding motif, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Mitochondrion matrix: P11914 P10507; Mitochondrion inner membrane: P04037
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 417893.63

構造登録者

Taylor, A.B.,Smith, B.S.,Kitada, S.,Kojima, K.,Miyaura, H.,Otwinowski, Z.,Ito, A.,Deisenhofer, J. (登録日: 2000-12-21, 公開日: 2001-07-11, 最終更新日: 2023-08-09)

主引用文献

Taylor, A.B.,Smith, B.S.,Kitada, S.,Kojima, K.,Miyaura, H.,Otwinowski, Z.,Ito, A.,Deisenhofer, J.
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences.
Structure, 9:615-625, 2001

PubMed Abstract: Mitochondrial processing peptidase (MPP) is a metalloendopeptidase that cleaves the N-terminal signal sequences of nuclear-encoded proteins targeted for transport from the cytosol to the mitochondria. Mitochondrial signal sequences vary in length and sequence, but each is cleaved at a single specific site by MPP. The cleavage sites typically contain an arginine at position -2 (in the N-terminal portion) from the scissile peptide bond in addition to other distal basic residues, and an aromatic residue at position +1. Mitochondrial import machinery recognizes amphiphilic helical conformations in signal sequences. However, it is unclear how MPP specifically recognizes diverse presequence substrates.

PubMed: 11470436
DOI: 10.1016/S0969-2126(01)00621-9

実験手法

X-RAY DIFFRACTION (2.7 Å)