View source for 7d5p


==Structure of NorC transporter in an outward-open conformation in complex with a single-chain Indian camelid antibody==
<StructureSection load='7d5p' size='340' side='right'caption='[[7d5p]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7d5p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D5P 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]] 3.65&#8491;</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7d5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d5p OCA], [https://pdbe.org/7d5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d5p RCSB], [https://www.ebi.ac.uk/pdbsum/7d5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d5p ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transporters play vital roles in acquiring antimicrobial resistance among pathogenic bacteria. In this study, we report the X-ray structure of NorC, a 14-transmembrane major facilitator superfamily member that is implicated in fluoroquinolone resistance in drug-resistant Staphylococcus aureus strains, at a resolution of 3.6 A. The NorC structure was determined in complex with a single-domain camelid antibody that interacts at the extracellular face of the transporter and stabilizes it in an outward-open conformation. The complementarity determining regions of the antibody enter and block solvent access to the interior of the vestibule, thereby inhibiting alternating-access. NorC specifically interacts with an organic cation, tetraphenylphosphonium, although it does not demonstrate an ability to transport it. The interaction is compromised in the presence of NorC-antibody complex, consequently establishing a strategy to detect and block NorC and related transporters through the use of single-domain camelid antibodies.

Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody.,Kumar S, Athreya A, Gulati A, Nair RM, Mahendran I, Ranjan R, Penmatsa A Commun Biol. 2021 Jul 5;4(1):836. doi: 10.1038/s42003-021-02357-x. PMID:34226658<ref>PMID:34226658</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7d5p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Camelus dromedarius]]
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus COL]]
[[Category: Athreya A]]
[[Category: Kumar S]]
[[Category: Penmatsa A]]