|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6h95' size='340' side='right'caption='[[6h95]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6h95' size='340' side='right'caption='[[6h95]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6h95]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_oxytocus_perniciosus"_flugge_1886 "bacillus oxytocus perniciosus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H95 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H95 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6h95]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H95 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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">albA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=571 "Bacillus oxytocus perniciosus" Flugge 1886])</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=6h95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h95 OCA], [http://pdbe.org/6h95 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h95 RCSB], [http://www.ebi.ac.uk/pdbsum/6h95 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h95 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=6h95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h95 OCA], [https://pdbe.org/6h95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h95 RCSB], [https://www.ebi.ac.uk/pdbsum/6h95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h95 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8KRS7_KLEOX Q8KRS7_KLEOX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus oxytocus perniciosus flugge 1886]] | + | [[Category: Klebsiella oxytoca]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Koehnke, J]] | + | [[Category: Koehnke J]] |
| - | [[Category: Sikandar, A]] | + | [[Category: Sikandar A]] |
| - | [[Category: Albicidin binding protein]]
| + | |
| - | [[Category: Albicidin resistance protein]]
| + | |
| Structural highlights
Function
Q8KRS7_KLEOX
Publication Abstract from PubMed
To combat the rise of antimicrobial resistance, the discovery of new antibiotics is paramount. Albicidin and cystobactamid are related natural product antibiotics with potent activity against Gram-positive and, crucially, Gram-negative pathogens. AlbA has been reported to neutralize albicidin by binding it with nanomolar affinity. To understand this potential resistance mechanism, we determined structures of AlbA and its complex with albicidin. The structures revealed AlbA to be comprised of two domains, each unexpectedly resembling the multiantibiotic neutralizing protein TipA. Binding of the long albicidin molecule was shared pseudosymmetrically between the two domains. The structure also revealed an unexpected chemical modification of albicidin, which we demonstrate to be promoted by AlbA, and to reduce albicidin potency; we propose a mechanism for this reaction. Overall, our findings suggest that AlbA arose through internal duplication in an ancient TipA-like gene, leading to a new binding scaffold adapted to the sequestration of long-chain antibiotics.
Adaptation of a Bacterial Multidrug Resistance System Revealed by the Structure and Function of AlbA.,Sikandar A, Cirnski K, Testolin G, Volz C, Bronstrup M, Kalinina OV, Muller R, Koehnke J J Am Chem Soc. 2018 Dec 5;140(48):16641-16649. doi: 10.1021/jacs.8b08895. Epub, 2018 Nov 27. PMID:30422653[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sikandar A, Cirnski K, Testolin G, Volz C, Bronstrup M, Kalinina OV, Muller R, Koehnke J. Adaptation of a Bacterial Multidrug Resistance System Revealed by the Structure and Function of AlbA. J Am Chem Soc. 2018 Dec 5;140(48):16641-16649. doi: 10.1021/jacs.8b08895. Epub, 2018 Nov 27. PMID:30422653 doi:http://dx.doi.org/10.1021/jacs.8b08895
|
