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4DK1

Crystal Structure of MacA-MexA chimeric protein, containing the Pseudomonas aeruginosa MexA alpha-hairpin domain.

Summary for 4DK1
Entry DOI10.2210/pdb4dk1/pdb
Related4DK0
DescriptorPutative MacA, Multidrug resistance protein mexA (1 entity in total)
Functional Keywordsalpha-hairpin, lipoyl, beta-barrel domains, periplasmic protein, membrane protein
Biological sourceAggregatibacter actinomycetemcomitans
More
Total number of polymer chains4
Total formula weight147373.12
Authors
Xu, Y.,Ha, N.C. (deposition date: 2012-02-03, release date: 2012-03-07, Last modification date: 2024-11-13)
Primary citationXu, Y.,Moeller, A.,Jun, S.Y.,Le, M.,Yoon, B.Y.,Kim, J.S.,Lee, K.,Ha, N.C.
Assembly and channel opening of outer membrane protein in tripartite drug efflux pumps of Gram-negative bacteria.
J.Biol.Chem., 287:11740-11750, 2012
Cited by
PubMed Abstract: Gram-negative bacteria are capable of expelling diverse xenobiotic substances from within the cell by use of three-component efflux pumps in which the energy-activated inner membrane transporter is connected to the outer membrane channel protein via the membrane fusion protein. In this work, we describe the crystal structure of the membrane fusion protein MexA from the Pseudomonas aeruginosa MexAB-OprM pump in the hexameric ring arrangement. Electron microscopy study on the chimeric complex of MexA and the outer membrane protein OprM reveals that MexA makes a tip-to-tip interaction with OprM, which suggests a docking model for MexA and OprM. This docking model agrees well with genetic results and depicts detailed interactions. Opening of the OprM channel is accompanied by the simultaneous exposure of a protein structure resembling a six-bladed cogwheel, which intermeshes with the complementary cogwheel structure in the MexA hexamer. Taken together, we suggest an assembly and channel opening model for the MexAB-OprM pump. This study provides a better understanding of multidrug resistance in Gram-negative bacteria.
PubMed: 22308040
DOI: 10.1074/jbc.M111.329375
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.499 Å)
Structure validation

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