Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system.

ATP-Binding Cassette Transporters / genetics Bacterial Proteins / chemistry Biological Transport Cell Membrane / metabolism Crystallography, X-Ray Gram-Negative Bacteria / metabolism Membrane Proteins / genetics Membrane Transport Proteins / chemistry Models, Biological Multiprotein Complexes / genetics Periplasm / metabolism Phospholipids / metabolism Protein Binding Protein Conformation, beta-Strand

Journal

Nature microbiology

ISSN: 2058-5276

Titre abrégé: Nat Microbiol

Pays: England

ID NLM: 101674869

Informations de publication

Date de publication:
10 2019

Historique:

received: 09 08 2018

accepted: 03 05 2019

pubmed: 27 6 2019

medline: 21 1 2020

entrez: 26 6 2019

Statut: ppublish

Résumé

The Mla pathway is believed to be involved in maintaining the asymmetrical Gram-negative outer membrane via retrograde phospholipid transport. The pathway is composed of three components: the outer membrane MlaA-OmpC/F complex, a soluble periplasmic protein, MlaC, and the inner membrane ATPase, MlaFEDB complex. Here, we solve the crystal structure of MlaC in its phospholipid-free closed apo conformation, revealing a pivoting β-sheet mechanism that functions to open and close the phospholipid-binding pocket. Using the apo form of MlaC, we provide evidence that the inner-membrane MlaFEDB machinery exports phospholipids to MlaC in the periplasm. Furthermore, we confirm that the phospholipid export process occurs through the MlaD component of the MlaFEDB complex and that this process is independent of ATP. Our data provide evidence of an apparatus for lipid export away from the inner membrane and suggest that the Mla pathway may have a role in anterograde phospholipid transport.

Identifiants

DOI: 10.1038/s41564-019-0481-y PMID: 31235958

pubmed: 31235958

doi: 10.1038/s41564-019-0481-y

pii: 10.1038/s41564-019-0481-y

doi:

Substances chimiques

ATP-Binding Cassette Transporters 0

Bacterial Proteins 0

Membrane Proteins 0

Membrane Transport Proteins 0

Multiprotein Complexes 0

Phospholipids 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

Pagination

1692-1705

Subventions

Organisme : Biotechnology and Biological Sciences Research Council

ID : BB/P009840/1

Pays : United Kingdom

Organisme : Wellcome Trust

ID : 208400/Z/17/Z

Pays : United Kingdom

Commentaires et corrections

Type : CommentIn

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