5dl8: Difference between revisions
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''' | ==Crystal structure of Acinetobacter baumannii OccAB4== | ||
<StructureSection load='5dl8' size='340' side='right' caption='[[5dl8]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dl8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DL8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl8 OCA], [http://pdbe.org/5dl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dl8 RCSB], [http://www.ebi.ac.uk/pdbsum/5dl8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:26805524</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5dl8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Basle, A]] | [[Category: Basle, A]] | ||
[[Category: Berg, B van den]] | |||
[[Category: Zahn, M]] | [[Category: Zahn, M]] | ||
[[Category: Acinetobacter baumannii]] | |||
[[Category: Antibiotic uptake]] | |||
[[Category: Beta-barrel]] | |||
[[Category: Membrane protein]] | |||
[[Category: Outer membrane protein]] | |||
Revision as of 18:42, 3 February 2016
Crystal structure of Acinetobacter baumannii OccAB4Crystal structure of Acinetobacter baumannii OccAB4
Structural highlights
Publication Abstract from PubMedBacterial 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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