6RWT

Crystal structure of the Cbp3 homolog from Brucella abortus

6RWT の概要

• エントリーDOI: 10.2210/pdb6rwt/pdb
• 分子名称: Ubiquinol-cytochrome C chaperone, MAGNESIUM ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: respiratory chain, complex iii, assembly factor, mitochondrial translation, chaperone
• 由来する生物種: Brucella abortus NCTC 8038
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21109.84

構造登録者

Masuyer, G.,Ndi, M.,Ott, M.,Stenmark, P. (登録日: 2019-06-06, 公開日: 2019-09-18, 最終更新日: 2024-05-15)

主引用文献

Ndi, M.,Masuyer, G.,Dawitz, H.,Carlstrom, A.,Michel, M.,Elofsson, A.,Rapp, M.,Stenmark, P.,Ott, M.
Structural basis for the interaction of the chaperone Cbp3 with newly synthesized cytochromebduring mitochondrial respiratory chain assembly.
J.Biol.Chem., 294:16663-16671, 2019

PubMed Abstract: Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3-Cbp6 chaperone complex binds newly synthesized cytochrome and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains: an N-terminal domain present in mitochondrial Cbp3 homologs and a highly conserved C-terminal domain comprising a ubiquinol-cytochrome chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4 Å resolution, revealing a unique all-helical fold. This structure allowed mapping of the interaction sites of yeast Cbp3 with Cbp6 and cytochrome via site-specific photo-cross-linking. We propose that mitochondrial Cbp3 homologs carry an N-terminal extension that positions the conserved C-terminal domain at the ribosomal tunnel exit for an efficient interaction with its substrate, the newly synthesized cytochrome protein.

PubMed: 31537648
DOI: 10.1074/jbc.RA119.010483

実験手法

X-RAY DIFFRACTION (1.42 Å)