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| | <StructureSection load='4p3y' size='340' side='right'caption='[[4p3y]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='4p3y' size='340' side='right'caption='[[4p3y]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p3y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciby Aciby] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p3y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_AYE Acinetobacter baumannii AYE] and [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbA, ABAYE3833 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=509173 ACIBY])</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=4p3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3y OCA], [https://pdbe.org/4p3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3y RCSB], [https://www.ebi.ac.uk/pdbsum/4p3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3y ProSAT]</span></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=4p3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3y OCA], [http://pdbe.org/4p3y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3y RCSB], [http://www.ebi.ac.uk/pdbsum/4p3y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C6EGC5_ECOBD C6EGC5_ECOBD]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity).[RuleBase:RU000325][HAMAP-Rule:MF_00118] | + | [https://www.uniprot.org/uniprot/B0V5X3_ACIBY B0V5X3_ACIBY] |
| | <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: Aciby]] | + | [[Category: Acinetobacter baumannii AYE]] |
| - | [[Category: Escherichia coli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Martin, J L]] | + | [[Category: Martin JL]] |
| - | [[Category: Premkumar, L]] | + | [[Category: Premkumar L]] |
| - | [[Category: Anti-biofilm formation]]
| + | |
| - | [[Category: Antivirulence]]
| + | |
| - | [[Category: Bacterial infection]]
| + | |
| - | [[Category: Disulfide bond formation]]
| + | |
| - | [[Category: Disulfide oxidase dsba]]
| + | |
| - | [[Category: Multidrug resistance]]
| + | |
| - | [[Category: Thioredoxin related]]
| + | |
| - | [[Category: Translation-oxidoreductase complex]]
| + | |
| Structural highlights
Function
B0V5X3_ACIBY
Publication Abstract from PubMed
The multidrug resistant bacterium Acinetobacter baumannii is a significant cause of nosocomial infection. Biofilm formation - that requires both disulfide bond forming and chaperone-usher pathways - is a major virulence trait in this bacterium. Our biochemical characterizations show that the periplasmic A. baumannii DsbA (AbDsbA) enzyme has an oxidizing redox potential and dithiol oxidase activity. We found an unexpected non-covalent interaction between AbDsbA and the highly conserved prokaryotic elongation factor, EF-Tu. EF-Tu is a cytoplasmic protein but has been localized extracellularly in many bacterial pathogens. The crystal structure of this complex revealed that the EF-Tu switch I region binds to the non-catalytic surface of AbDsbA. Though the physiological and pathological significance of a DsbA/EF-Tu association is unknown, peptides derived from the EF-Tu switch I region bound to AbDsbA with submicromolar affinity. We also identified a 7-residue DsbB-derived peptide that bound to AbDsbA with low micromolar affinity. Further characterization confirmed that the EF-Tu and DsbB derived peptides bind at two distinct sites. These data point to the possibility that the non-catalytic surface of DsbA is a potential substrate or regulatory protein interaction site. The two peptides identified in this work, together with the newly characterized interaction site, provide a novel starting point for inhibitor design targeting AbDsbA.
Structure of the Acinetobacter Baumannii Dithiol Oxidase DsbA Bound to EF-Tu Reveals a Novel Protein Interaction Site.,Premkumar L, Kurth F, Duprez W, Groftehauge MK, King GJ, Halili MA, Heras B, Martin JL J Biol Chem. 2014 May 23. pii: jbc.M114.571737. PMID:24860094[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Premkumar L, Kurth F, Duprez W, Groftehauge MK, King GJ, Halili MA, Heras B, Martin JL. Structure of the Acinetobacter Baumannii Dithiol Oxidase DsbA Bound to EF-Tu Reveals a Novel Protein Interaction Site. J Biol Chem. 2014 May 23. pii: jbc.M114.571737. PMID:24860094 doi:http://dx.doi.org/10.1074/jbc.M114.571737
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