Structure-Function Characterization of the Conserved Regulatory Mechanism of the Escherichia coli M48 Metalloprotease BepA.

Amino Acid Sequence Bacterial Outer Membrane Proteins / chemistry Crystallography, X-Ray Escherichia coli / enzymology Escherichia coli Proteins / chemistry Metalloproteases / chemistry Permeability Sensitivity and Specificity Structure-Activity Relationship
BAM complex BepA Escherichia coli LptD M48 metalloprotease lipopolysaccharide outer membrane protease structure

Journal

Journal of bacteriology
ISSN: 1098-5530
Titre abrégé: J Bacteriol
Pays: United States
ID NLM: 2985120R

Informations de publication

Date de publication:
18 12 2020
Historique:
received: 30 07 2020
accepted: 18 10 2020
pubmed: 28 10 2020
medline: 13 5 2021
entrez: 27 10 2020
Statut: epublish

Résumé

The asymmetric Gram-negative outer membrane (OM) is the first line of defense for bacteria against environmental insults and attack by antimicrobials. The key component of the OM is lipopolysaccharide, which is transported to the surface by the essential lipopolysaccharide transport (Lpt) system. Correct folding of the Lpt system component LptD is regulated by a periplasmic metalloprotease, BepA. Here, we present the crystal structure of BepA from

Identifiants

DOI: 10.1128/JB.00434-20 PMID: 33106348 PMC: PMC7950410
pubmed: 33106348
pii: JB.00434-20
doi: 10.1128/JB.00434-20
pmc: PMC7950410
pii:
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
BamA protein, E coli 0
Escherichia coli Proteins 0
BepA protein, E coli EC 3.4.-
Metalloproteases EC 3.4.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
Pays : United Kingdom
Organisme : Medical Research Council
Pays : United Kingdom

Informations de copyright

Copyright © 2020 Bryant et al.

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Auteurs

Jack A Bryant (JA)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom j.a.bryant@bham.ac.uk i.henderson@imb.uq.edu.au.

Ian T Cadby (IT)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Zhi-Soon Chong (ZS)

Department of Chemistry, National University of Singapore, Singapore, Singapore.

Gabriela Boelter (G)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Yanina R Sevastsyanovich (YR)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Faye C Morris (FC)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.
ORCID: 0000-0002-9021-0452

Adam F Cunningham (AF)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.
ORCID: 0000-0003-0248-964X

George Kritikos (G)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Richard W Meek (RW)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Manuel Banzhaf (M)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Shu-Sin Chng (SS)

Department of Chemistry, National University of Singapore, Singapore, Singapore.
ORCID: 0000-0001-5466-7183

Andrew L Lovering (AL)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

Ian R Henderson (IR)

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom j.a.bryant@bham.ac.uk i.henderson@imb.uq.edu.au.
Institute for Molecular Bioscience, University of Queensland, St. Lucia, Australia.
ORCID: 0000-0002-9954-4977

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Classifications MeSH

questionsmedicales.fr › Sciences de l'information › Sources d'information › Services d'information › Documentation › Données de séquences moléculaires › Séquence d'acides aminés › Structure-Function Characterization of the...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de la membrane externe bactérienne › Structure-Function Characterization of the...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Cristallographie aux rayons X › Structure-Function Characterization of the...
questionsmedicales.fr › Bactéries › Proteobacteria › Gammaproteobacteria › Enterobacteriaceae › Escherichia › Escherichia coli › Structure-Function Characterization of the...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines bactériennes › Protéines Escherichia coli › Structure-Function Characterization of the...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Peptide hydrolases › Metalloproteases › Structure-Function Characterization of the...
questionsmedicales.fr › Phénomènes chimiques › Perméabilité › Structure-Function Characterization of the...
questionsmedicales.fr › Environnement et santé publique › Santé publique › Méthodes épidémiologiques › Statistiques comme sujet › Sensibilité et spécificité › Structure-Function Characterization of the...
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Relation structure-activité › Structure-Function Characterization of the...