The assembly of β-barrel outer membrane proteins.
Journal
Current opinion in microbiology
ISSN: 1879-0364
Titre abrégé: Curr Opin Microbiol
Pays: England
ID NLM: 9815056
Informations de publication
Date de publication:
04 2021
04 2021
Historique:
received:
15
12
2020
revised:
17
01
2021
accepted:
22
01
2021
pubmed:
10
2
2021
medline:
16
10
2021
entrez:
9
2
2021
Statut:
ppublish
Résumé
The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts contain β-barrel integral membrane proteins. In bacteria, the five-protein β-barrel assembly machine (Bam) accelerates the folding and membrane integration of these proteins. The central component of the machine, BamA, contains a β-barrel domain that can adopt a lateral-open state with its N-terminal and C-terminal β-strands unpaired. Recently, strategies have been developed to capture β-barrel folding intermediates on the Bam complex. Biochemical and structural studies provide support for a model in which substrates assemble at the lateral opening of BamA. In this model, the N-terminal β-strand of BamA captures the C-terminal β-strand of substrates by hydrogen bonding to allow their directional folding and subsequent release into the membrane.
Identifiants
pubmed: 33561734
pii: S1369-5274(21)00015-1
doi: 10.1016/j.mib.2021.01.009
pmc: PMC7988294
mid: NIHMS1667688
pii:
doi:
Substances chimiques
Bacterial Outer Membrane Proteins
0
BamA protein, E coli
0
Escherichia coli Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
16-23Subventions
Organisme : NIAID NIH HHS
ID : R01 AI081059
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM066174
Pays : United States
Informations de copyright
Copyright © 2021 Elsevier Ltd. All rights reserved.
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