7F03

Cytochrome c-type biogenesis protein CcmABCD from E. coli in complex with ANP

7F03 の概要

• エントリーDOI: 10.2210/pdb7f03/pdb
• EMDBエントリー: 31395
• 分子名称: Cytochrome c biogenesis ATP-binding export protein CcmA, Heme exporter protein B, Heme exporter protein C, ... (8 entities in total)
• 機能のキーワード: atp-binding exporter, heme transmembrane transporter, cytochrome c biogenesis protein., membrane protein
• 由来する生物種: Escherichia coli BL21(DE3); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 130899.21

構造登録者

Li, J.,Zheng, W.,Gu, M.,Zhang, K.,Zhu, J.P. (登録日: 2021-06-03, 公開日: 2022-11-09, 最終更新日: 2024-06-12)

主引用文献

Li, J.,Zheng, W.,Gu, M.,Han, L.,Luo, Y.,Yu, K.,Sun, M.,Zong, Y.,Ma, X.,Liu, B.,Lowder, E.P.,Mendez, D.L.,Kranz, R.G.,Zhang, K.,Zhu, J.
Structures of the CcmABCD heme release complex at multiple states.
Nat Commun, 13:6422-6422, 2022

PubMed Abstract: Cytochromes c use heme as a cofactor to carry electrons in respiration and photosynthesis. The cytochrome c maturation system I, consisting of eight membrane proteins (CcmABCDEFGH), results in the attachment of heme to cysteine residues of cytochrome c proteins. Since all c-type cytochromes are periplasmic, heme is first transported to a periplasmic heme chaperone, CcmE. A large membrane complex, CcmABCD has been proposed to carry out this transport and linkage to CcmE, yet the structural basis and mechanisms underlying the process are unknown. We describe high resolution cryo-EM structures of CcmABCD in an unbound form, in complex with inhibitor AMP-PNP, and in complex with ATP and heme. We locate the ATP-binding site in CcmA and the heme-binding site in CcmC. Based on our structures combined with functional studies, we propose a hypothetic model of heme trafficking, heme transfer to CcmE, and ATP-dependent release of holoCcmE from CcmABCD. CcmABCD represents an ABC transporter complex using the energy of ATP hydrolysis for the transfer of heme from one binding partner (CcmC) to another (CcmE).

PubMed: 36307425
DOI: 10.1038/s41467-022-34136-5

実験手法

ELECTRON MICROSCOPY (3.29 Å)