6ZMQ

Cytochrome c Heme Lyase CcmF

6ZMQ の概要

• エントリーDOI: 10.2210/pdb6zmq/pdb
• 分子名称: Cytochrome C-type biogenesis protein ccmF, PROTOPORPHYRIN IX CONTAINING FE, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total)
• 機能のキーワード: heme lyase cytochrome c maturation membrane protein cytochrome, membrane protein
• 由来する生物種: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77273.72

構造登録者

Brausemann, A.,Einsle, O. (登録日: 2020-07-03, 公開日: 2021-05-19, 最終更新日: 2024-05-15)

主引用文献

Brausemann, A.,Zhang, L.,Ilcu, L.,Einsle, O.
Architecture of the membrane-bound cytochrome c heme lyase CcmF.
Nat.Chem.Biol., 17:800-805, 2021

PubMed Abstract: The covalent attachment of one or multiple heme cofactors to cytochrome c protein chains enables cytochrome c proteins to be used in electron transfer and redox catalysis in extracytoplasmic environments. A dedicated heme maturation machinery, whose core component is a heme lyase, scans nascent peptides after Sec-dependent translocation for CXCH-binding motifs. Here we report the three-dimensional (3D) structure of the heme lyase CcmF, a 643-amino acid integral membrane protein, from Thermus thermophilus. CcmF contains a heme b cofactor at the bottom of a large cavity that opens toward the extracellular side to receive heme groups from the heme chaperone CcmE for cytochrome maturation. A surface groove on CcmF may guide the extended apoprotein to heme attachment at or near a loop containing the functionally essential WXWD motif, which is situated above the putative cofactor binding pocket. The structure suggests heme delivery from within the membrane, redefining the role of the chaperone CcmE.

PubMed: 33958791
DOI: 10.1038/s41589-021-00793-8

実験手法

X-RAY DIFFRACTION (2.67 Å)