Structural basis of membrane machines that traffick and attach heme to cytochromes.
bioenergetics
biogenesis
cytochrome
cytochrome c
heme
heme attachment
leaflet
molecular machine
structure
transport
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
received:
31
08
2023
revised:
04
10
2023
accepted:
06
10
2023
medline:
27
11
2023
pubmed:
13
10
2023
entrez:
12
10
2023
Statut:
ppublish
Résumé
We evaluate cryoEM and crystal structures of two molecular machines that traffick heme and attach it to cytochrome c (cyt c), the second activity performed by a cyt c synthase. These integral membrane proteins, CcsBA and CcmF/H, both covalently attach heme to cyt c, but carry it out via different mechanisms. A CcsB-CcsA complex transports heme through a channel to its external active site, where it forms two thioethers between reduced (Fe
Identifiants
pubmed: 37827288
pii: S0021-9258(23)02360-8
doi: 10.1016/j.jbc.2023.105332
pmc: PMC10663686
pii:
doi:
Substances chimiques
Cytochromes c
9007-43-6
Heme
42VZT0U6YR
Membrane Proteins
0
Bacterial Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105332Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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