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| | <StructureSection load='6eus' size='340' side='right'caption='[[6eus]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6eus' size='340' side='right'caption='[[6eus]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6eus]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EUS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6eus]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EUS FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABUW_0826, B4R90_15245, CAS84_19480, CAT05_14765, CBI29_03066, IX87_10345 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6eus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eus OCA], [http://pdbe.org/6eus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eus RCSB], [http://www.ebi.ac.uk/pdbsum/6eus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eus ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6eus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eus OCA], [https://pdbe.org/6eus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eus RCSB], [https://www.ebi.ac.uk/pdbsum/6eus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eus ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0B9X9I7_ACIBA A0A0B9X9I7_ACIBA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aciba]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Berg, B van den]] | |
| - | [[Category: Zahn, M]] | |
| | [[Category: Acinetobacter baumannii]] | | [[Category: Acinetobacter baumannii]] |
| - | [[Category: Membrane protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Outer membrane protein]] | + | [[Category: Zahn M]] |
| | + | [[Category: Van den Berg B]] |
| Structural highlights
Function
A0A0B9X9I7_ACIBA
Publication Abstract from PubMed
Research efforts to discover potential new antibiotics for Gram-negative bacteria suffer from high attrition rates due to the synergistic action of efflux systems and the limited permeability of the outer membrane (OM). One strategy to overcome the OM permeability barrier is to identify small molecules that are natural substrates for abundant OM channels and use such compounds as scaffolds for the design of efficiently permeating antibacterials. Here we present a multidisciplinary approach to identify such potential small-molecule scaffolds. Focusing on the pathogenic bacterium Acinetobacter baumannii, we use OM proteomics to identify DcaP as the most abundant channel during infection in rodents. The X-ray crystal structure of DcaP reveals a trimeric, porin-like structure and suggests that dicarboxylic acids are potential transport substrates. Electrophysiological experiments and all-atom molecular dynamics simulations confirm this notion and provide atomistic information on likely permeation pathways and energy barriers for several small molecules, including a clinically relevant beta-lactamase inhibitor.
A Multidisciplinary Approach toward Identification of Antibiotic Scaffolds for Acinetobacter baumannii.,Bhamidimarri SP, Zahn M, Prajapati JD, Schleberger C, Soderholm S, Hoover J, West J, Kleinekathofer U, Bumann D, Winterhalter M, van den Berg B Structure. 2019 Feb 5;27(2):268-280.e6. doi: 10.1016/j.str.2018.10.021. Epub 2018, Dec 13. PMID:30554842[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bhamidimarri SP, Zahn M, Prajapati JD, Schleberger C, Soderholm S, Hoover J, West J, Kleinekathofer U, Bumann D, Winterhalter M, van den Berg B. A Multidisciplinary Approach toward Identification of Antibiotic Scaffolds for Acinetobacter baumannii. Structure. 2019 Feb 5;27(2):268-280.e6. doi: 10.1016/j.str.2018.10.021. Epub 2018, Dec 13. PMID:30554842 doi:http://dx.doi.org/10.1016/j.str.2018.10.021
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