View source for 6h96


==AlbA-albicidin complex, albicidin resistance protein==
<StructureSection load='6h96' size='340' side='right'caption='[[6h96]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6h96]] is a 2 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=6H96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H96 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FWE:4-[[4-[[4-[(3~{S})-5-azanyl-3-[[4-[[(~{E})-3-(4-hydroxyphenyl)-2-methyl-prop-2-enoyl]amino]phenyl]carbonylamino]-2-oxidanylidene-3~{H}-pyrrol-1-yl]phenyl]carbonylamino]-3-methoxy-2-oxidanyl-phenyl]carbonylamino]-3-methoxy-2-oxidanyl-benzoic+acid'>FWE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6h96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h96 OCA], [https://pdbe.org/6h96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h96 RCSB], [https://www.ebi.ac.uk/pdbsum/6h96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h96 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8KRS7_KLEOX Q8KRS7_KLEOX] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:30422653</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6h96" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella oxytoca]]
[[Category: Large Structures]]
[[Category: Koehnke J]]
[[Category: Sikandar A]]