4dk0

Crystal structure of MacA from Actinobacillus actinomycetemcomitans

spinqualitylabelsall models 4dk0, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4dk0 is a 1 chain structure with sequence from Aggregatibacter actinomycetemcomitans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q2EHL9_AGGAC] Publication Abstract from PubMed 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. Assembly and channel opening of outer membrane protein in tripartite drug efflux pumps of Gram-negative bacteria.,Xu Y, Moeller A, Jun SY, Le M, Yoon BY, Kim JS, Lee K, Ha NC J Biol Chem. 2012 Apr 6;287(15):11740-50. Epub 2012 Feb 3. PMID:22308040 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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