6gie

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'''Unreleased structure'''
 
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The entry 6gie is ON HOLD until Paper Publication
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==Crystal structure of the Acinetobacter baumannii outer membrane protein Omp33==
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<StructureSection load='6gie' size='340' side='right' caption='[[6gie]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6gie]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GIE FirstGlance]. <br>
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</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></td></tr>
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<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=6gie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gie OCA], [http://pdbe.org/6gie PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gie RCSB], [http://www.ebi.ac.uk/pdbsum/6gie PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gie 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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Acinetobacter baumannii is becoming a major threat to human health due to its multidrug resistance. This is owing in a large part to the low permeability of its outer membrane (OM), which prevents high internal antibiotic concentrations and makes antibiotic-resistance mechanisms more effective. To exploit OM channels as potential delivery vehicles for future antibiotics, structural information is required. One abundant OM protein in A. baumannii is Omp33. This protein has been reported to be important for the in vivo fitness and virulence of A. baumannii, but its structure is not known. Here, the X-ray crystal structure of Omp33 is reported at a resolution of 2.1 A. Omp33 has a 14-beta-stranded barrel without stable extracellular loop constrictions. Instead, an extended and unusual periplasmic turn connecting beta-strands 2 and 3 is present, which folds into the pore lumen and completely blocks the aqueous channel. The Omp33 structure helps in understanding how A. baumannii OM proteins contribute to the low permeability of the cell envelope of this bacterium and suggests that Omp33 might function as a gated channel.
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Authors:
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Crystal structure of the Acinetobacter baumannii outer membrane protein Omp33.,Abellon-Ruiz J, Zahn M, Basle A, van den Berg B Acta Crystallogr D Struct Biol. 2018 Sep 1;74(Pt 9):852-860. doi:, 10.1107/S205979831800904X. Epub 2018 Sep 3. PMID:30198896<ref>PMID:30198896</ref>
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Description:
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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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<div class="pdbe-citations 6gie" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Abellon-Ruiz, J]]
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[[Category: Basle, A]]
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[[Category: Berg, B van den]]
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[[Category: Zahn, M]]
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[[Category: Channel]]
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[[Category: Membrane protein]]

Revision as of 19:57, 19 September 2018

Crystal structure of the Acinetobacter baumannii outer membrane protein Omp33

6gie, resolution 2.10Å

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