5dl6

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'''Unreleased structure'''
 
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The entry 5dl6 is ON HOLD until Paper Publication
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==Crystal structure of Acinetobacter baumannii OccAB2==
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<StructureSection load='5dl6' size='340' side='right'caption='[[5dl6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5dl6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_AB307-0294 Acinetobacter baumannii AB307-0294]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DL6 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl6 OCA], [https://pdbe.org/5dl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dl6 RCSB], [https://www.ebi.ac.uk/pdbsum/5dl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dl6 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Zahn, M., Basle, A., van den Berg, B.
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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>
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Description: Crystal structure of Acinetobacter baumannii OccAB2
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Van Den Berg, B]]
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<div class="pdbe-citations 5dl6" style="background-color:#fffaf0;"></div>
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[[Category: Basle, A]]
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== References ==
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[[Category: Zahn, M]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Acinetobacter baumannii AB307-0294]]
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[[Category: Large Structures]]
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[[Category: Basle A]]
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[[Category: Zahn M]]
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[[Category: Van den Berg B]]

Current revision

Crystal structure of Acinetobacter baumannii OccAB2

PDB ID 5dl6

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