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8BVQ

E. coli BAM complex (BamABCDE) bound to darobactin B

Summary for 8BVQ
Entry DOI10.2210/pdb8bvq/pdb
EMDB information16268
Related PRD IDPRD_002342
DescriptorOuter membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (6 entities in total)
Functional Keywordsouter membrane protein, protein folding, antibiotic, beta barrel, membrane protein
Biological sourceEscherichia coli
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Total number of polymer chains6
Total formula weight201281.21
Authors
Horne, J.E.,Fenn, K.L.,Radford, S.E.,Ranson, N.A. (deposition date: 2022-12-05, release date: 2023-05-24, Last modification date: 2023-09-06)
Primary citationHaysom, S.F.,Machin, J.,Whitehouse, J.M.,Horne, J.E.,Fenn, K.,Ma, Y.,El Mkami, H.,Bohringer, N.,Schaberle, T.F.,Ranson, N.A.,Radford, S.E.,Pliotas, C.
Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells.
Angew.Chem.Int.Ed.Engl., 62:e202218783-e202218783, 2023
Cited by
PubMed: 37162386
DOI: 10.1002/anie.202218783
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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