5dl7: Difference between revisions

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-'''Unreleased structure'''
+==Crystal structure of Acinetobacter baumannii OccAB3==
+<StructureSection load='5dl7' size='340' side='right' caption='[[5dl7]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5dl7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DL7 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=5dl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl7 OCA], [http://pdbe.org/5dl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dl7 RCSB], [http://www.ebi.ac.uk/pdbsum/5dl7 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.
-The entry 5dl7 is ON HOLD  until Paper Publication
+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>
-Authors: Zahn, M., Basle, A., van den Berg, B.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of Acinetobacter baumannii OccAB3
+<div class="pdbe-citations 5dl7" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Van Den Berg, B]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Basle, A]]
+[[Category: Berg, B van den]]
 [[Category: Zahn, M]]
+[[Category: Acinetobacter baumannii]]
+[[Category: Antibiotic uptake]]
+[[Category: Beta-barrel]]
+[[Category: Membrane protein]]
+[[Category: Outer membrane protein]]