Formation of a β-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA.
Amino Acid Motifs
Bacterial Outer Membrane Proteins
/ chemistry
Binding Sites
Cell Membrane
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli
/ genetics
Escherichia coli Proteins
/ chemistry
Gene Expression
Genetic Vectors
/ chemistry
Models, Molecular
Mutation
Protein Binding
Protein Conformation, beta-Strand
Protein Folding
Protein Interaction Domains and Motifs
Recombinant Proteins
/ chemistry
Substrate Specificity
Bam complex
E. coli
beta barrel
biochemistry
chemical biology
gram-negative bacteria
infectious disease
membrane protein folding
microbiology
outer membrane
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
14 11 2019
14 11 2019
Historique:
received:
29
06
2019
accepted:
13
11
2019
pubmed:
15
11
2019
medline:
10
5
2020
entrez:
15
11
2019
Statut:
epublish
Résumé
The β-barrel assembly machine (Bam) complex in Gram-negative bacteria and its counterparts in mitochondria and chloroplasts fold and insert outer membrane β-barrel proteins. BamA, an essential component of the complex, is itself a β-barrel and is proposed to play a central role in assembling other barrel substrates. Here, we map the path of substrate insertion by the Bam complex using site-specific crosslinking to understand the molecular mechanisms that control β-barrel folding and release. We find that the C-terminal strand of the substrate is stably held by BamA and that the N-terminal strands of the substrate are assembled inside the BamA β-barrel. Importantly, we identify contacts between the assembling β-sheet and the BamA interior surface that determine the rate of substrate folding. Our results support a model in which the interior wall of BamA acts as a chaperone to catalyze β-barrel assembly.
Identifiants
pubmed: 31724945
doi: 10.7554/eLife.49787
pii: 49787
pmc: PMC6887485
doi:
pii:
Substances chimiques
Bacterial Outer Membrane Proteins
0
BamA protein, E coli
0
Escherichia coli Proteins
0
LptD protein, E coli
0
Recombinant Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : F31GM116210
Pays : United States
Organisme : National Institute of Allergy and Infectious Diseases
ID : T32AI132120
Pays : International
Organisme : Howard Hughes Medical Institute
ID : Hanna H Gray Postdoctoral Fellowship
Pays : United States
Organisme : National Institute of Allergy and Infectious Diseases
ID : AI081059
Pays : International
Organisme : NIAID NIH HHS
ID : T32 AI132120
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI081059
Pays : United States
Informations de copyright
© 2019, Lee et al.
Déclaration de conflit d'intérêts
JL, DT, TS, MM, IM, DK No competing interests declared
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