5dl7

Crystal structure of Acinetobacter baumannii OccAB3

spinqualitylabelsall models 5dl7, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dl7 is a 1 chain structure with sequence from Acinetobacter baumannii AB307-0294. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: C8E, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0D5YKR4_ACIBA Publication Abstract from PubMed Bacterial resistance against antibiotics is an increasing global health problem. In Gram-negative bacteria the low permeability of the outer membrane (OM) is a major factor contributing to resistance, making it important to understand channel-mediated small-molecule passage of the OM. Acinetobacter baumannii has five Occ (OM carboxylate channel) proteins, which collectively are of major importance for the entry of small molecules. To improve our understanding of the OM permeability of A. baumannii, we present here the X-ray crystal structures of four Occ proteins, renamed OccAB1 to OccAB4. In addition we have carried out a biochemical and biophysical characterization using electrophysiology and liposome swelling experiments, providing information on substrate specificities. We identify OccAB1 as having the largest pore of the Occ proteins with corresponding high rates of small-molecule uptake, and we suggest that the future design of efficient antibiotics should focus on scaffolds that can permeate efficiently through the OccAB1 channel. Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii.,Zahn M, Bhamidimarri SP, Basle A, Winterhalter M, van den Berg B Structure. 2016 Jan 20. pii: S0969-2126(15)00535-3. doi:, 10.1016/j.str.2015.12.009. PMID:26805524 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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