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5LJ7

Structure of Aggregatibacter actinomycetemcomitans MacB bound to ATP (P21)

Summary for 5LJ7
Entry DOI10.2210/pdb5lj7/pdb
DescriptorMacrolide export ATP-binding/permease protein MacB, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsmembrane protein, abc transporter, transport protein
Biological sourceAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans)
Cellular locationCell inner membrane ; Multi-pass membrane protein : Q2EHL8
Total number of polymer chains2
Total formula weight145292.38
Authors
Crow, A. (deposition date: 2016-07-18, release date: 2017-11-15, Last modification date: 2024-01-10)
Primary citationCrow, A.,Greene, N.P.,Kaplan, E.,Koronakis, V.
Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily.
Proc. Natl. Acad. Sci. U.S.A., 114:12572-12577, 2017
Cited by
PubMed Abstract: MacB is an ABC transporter that collaborates with the MacA adaptor protein and TolC exit duct to drive efflux of antibiotics and enterotoxin STII out of the bacterial cell. Here we present the structure of ATP-bound MacB and reveal precise molecular details of its mechanism. The MacB transmembrane domain lacks a central cavity through which substrates could be passed, but instead conveys conformational changes from one side of the membrane to the other, a process we term mechanotransmission. Comparison of ATP-bound and nucleotide-free states reveals how reversible dimerization of the nucleotide binding domains drives opening and closing of the MacB periplasmic domains via concerted movements of the second transmembrane segment and major coupling helix. We propose that the assembled tripartite pump acts as a molecular bellows to propel substrates through the TolC exit duct, driven by MacB mechanotransmission. Homologs of MacB that do not form tripartite pumps, but share structural features underpinning mechanotransmission, include the LolCDE lipoprotein trafficking complex and FtsEX cell division signaling protein. The MacB architecture serves as the blueprint for understanding the structure and mechanism of an entire ABC transporter superfamily and the many diverse functions it supports.
PubMed: 29109272
DOI: 10.1073/pnas.1712153114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.25 Å)
Structure validation

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