4ziv | pdb_00004ziv

Crystal structure of AcrB triple mutant in P21 space group

spinqualitylabelsall models 4ziv, resolution 3.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ziv is a 6 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.16Å Ligands: LMT, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity. Publication Abstract from PubMed Gram-negative bacteria such as E. coli use tripartite efflux pumps such as AcrAB-TolC to expel antibiotics and noxious compounds. A key feature of the inner membrane transporter component, AcrB, is a short stretch of residues known as the gate/switch loop that divides the proximal and distal substrate binding pockets. Amino acid substitutions of the gate loop are known to decrease antibiotic resistance conferred by AcrB. Here we present two new AcrB gate loop variants, the first stripped of its bulky side chains, and a second in which the gate loop is removed entirely. By determining the crystal structures of the variant AcrB proteins in the presence and absence of erythromycin and assessing their ability to confer erythromycin tolerance, we demonstrate that the gate loop is important for AcrB export activity but is not required for erythromycin binding. Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate.,Ababou A, Koronakis V PLoS One. 2016 Jul 12;11(7):e0159154. doi: 10.1371/journal.pone.0159154., eCollection 2016. PMID:27403665 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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