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6IC4

Cryo-EM structure of the A. baumannii MLA complex at 8.7 A resolution

Summary for 6IC4
Entry DOI10.2210/pdb6ic4/pdb
EMDB information0007
DescriptorToluene tolerance efflux transporter (ABC superfamily, PerI-bind), ABC transporter permease, ABC transporter ATP-binding protein, ... (4 entities in total)
Functional Keywordsmembrane protein antibiotic resistance abc transporter, protein transport
Biological sourceAcinetobacter baumannii
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Total number of polymer chains12
Total formula weight246316.62
Authors
Bergeron, J.R.,Kollman, J.M. (deposition date: 2018-12-02, release date: 2019-01-23, Last modification date: 2024-05-15)
Primary citationKamischke, C.,Fan, J.,Bergeron, J.,Kulasekara, H.D.,Dalebroux, Z.D.,Burrell, A.,Kollman, J.M.,Miller, S.I.
The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane.
Elife, 8:-, 2019
Cited by
PubMed Abstract: The outer membrane (OM) of Gram-negative bacteria serves as a selective permeability barrier that allows entry of essential nutrients while excluding toxic compounds, including antibiotics. The OM is asymmetric and contains an outer leaflet of lipopolysaccharides (LPS) or lipooligosaccharides (LOS) and an inner leaflet of glycerophospholipids (GPL). We screened transposon mutants and identified a number of mutants with OM defects, including an ABC transporter system homologous to the Mla system in We further show that this opportunistic, antibiotic-resistant pathogen uses this multicomponent protein complex and ATP hydrolysis at the inner membrane to promote GPL export to the OM. The broad conservation of the Mla system in Gram-negative bacteria suggests the system may play a conserved role in OM biogenesis. The importance of the Mla system to OM integrity and antibiotic sensitivity suggests that its components may serve as new antimicrobial therapeutic targets.
PubMed: 30638443
DOI: 10.7554/eLife.40171
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.7 Å)
Structure validation

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数据于2025-07-09公开中

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