7TCH

BceAB E169Q variant ATP-bound conformation

Summary for 7TCH

• Entry DOI: 10.2210/pdb7tch/pdb
• EMDB information: 25811 25812
• Descriptor: Bacitracin export permease protein BceB, Bacitracin export ATP-binding protein BceA, 4-amino-4-deoxy-1-O-[(S)-hydroxy{[(2E,6E,10Z,14Z,18Z,22E,26E,30E)-3,7,11,15,19,23,27,31,35-nonamethylhexatriaconta-2,6,10,14,18,22,26,30,34-nonaen-1-yl]oxy}phosphoryl]-alpha-L-arabinopyranose, ... (4 entities in total)
• Functional Keywords: bceab, bacitracin, transporter, transport protein
• Biological source: Bacillus subtilis subsp. subtilis str. 168; More
• Total number of polymer chains: 3
• Total formula weight: 132613.43

Authors

George, N.L.,Orlando, B.J. (deposition date: 2021-12-23, release date: 2022-04-06, Last modification date: 2024-02-28)

Primary citation

George, N.L.,Schilmiller, A.L.,Orlando, B.J.
Conformational snapshots of the bacitracin sensing and resistance transporter BceAB.
Proc.Natl.Acad.Sci.USA, 119:e2123268119-e2123268119, 2022

PubMed Abstract: SignificanceMany gram-positive organisms have evolved an elegant solution to sense and resist antimicrobial peptides that inhibit cell-wall synthesis. These organisms express an unusual "Bce-type" adenosine triphosphate-binding cassette (ABC) transporter that recognizes complexes formed between antimicrobial peptides and lipids involved in cell-wall biosynthesis. In this work, we provide the first structural snapshots of a Bce-type ABC transporter trapped in different conformational states. Our structures and associated biochemical data provide key insights into the novel target protection mechanism that these unusual ABC transporters use to sense and resist antimicrobial peptides. The studies described herein set the stage to begin developing a comprehensive molecular understanding of the diverse interactions between antimicrobial peptides and conserved resistance machinery found across most gram-positive organisms.

PubMed: 35349335
DOI: 10.1073/pnas.2123268119

Experimental method

ELECTRON MICROSCOPY (3.7 Å)