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| | ==Structure of MATE multidrug transporter DinF-BH== | | ==Structure of MATE multidrug transporter DinF-BH== |
| - | <StructureSection load='4lz6' size='340' side='right' caption='[[4lz6]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='4lz6' size='340' side='right'caption='[[4lz6]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lz6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bachd Bachd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LZ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LZ6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lz9|4lz9]]</td></tr> | + | </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=4lz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lz6 OCA], [https://pdbe.org/4lz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lz6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lz6 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BH2163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272558 BACHD])</td></tr>
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| - | <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=4lz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lz6 OCA], [http://pdbe.org/4lz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lz6 RCSB], [http://www.ebi.ac.uk/pdbsum/4lz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lz6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9KAX3_HALH5 Q9KAX3_HALH5] |
| | <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: Bachd]] | + | [[Category: Alkalihalobacillus halodurans C-125]] |
| - | [[Category: Guo, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Lu, M]] | + | [[Category: Guo Y]] |
| - | [[Category: Nie, R]] | + | [[Category: Lu M]] |
| - | [[Category: Radchenko, M]] | + | [[Category: Nie R]] |
| - | [[Category: Symersky, J]] | + | [[Category: Radchenko M]] |
| - | [[Category: Multidrug transporter]]
| + | [[Category: Symersky J]] |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
Q9KAX3_HALH5
Publication Abstract from PubMed
Multidrug and toxic compound extrusion (MATE) transporters contribute to multidrug resistance by coupling the efflux of drugs to the influx of Na(+) or H(+). Known structures of Na(+)-coupled, extracellular-facing MATE transporters from the NorM subfamily revealed 12 membrane-spanning segments related by a quasi-two-fold rotational symmetry and a multidrug-binding cavity situated near the membrane surface. Here we report the crystal structure of an H(+)-coupled MATE transporter from Bacillus halodurans and the DinF subfamily at 3.2-A resolution, unveiling a surprisingly asymmetric arrangement of 12 transmembrane helices. We also identified a membrane-embedded substrate-binding chamber by combining crystallographic and biochemical analyses. Our studies further suggested a direct competition between H(+) and substrate during DinF-mediated transport and implied how a MATE transporter alternates between its extracellular- and intracellular-facing conformations to propel multidrug extrusion. Collectively, our results demonstrated heretofore-unrecognized mechanistic diversity among MATE transporters.
Structural insights into H(+)-coupled multidrug extrusion by a MATE transporter.,Lu M, Radchenko M, Symersky J, Nie R, Guo Y Nat Struct Mol Biol. 2013 Nov;20(11):1310-7. doi: 10.1038/nsmb.2687. Epub 2013, Oct 20. PMID:24141706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu M, Radchenko M, Symersky J, Nie R, Guo Y. Structural insights into H(+)-coupled multidrug extrusion by a MATE transporter. Nat Struct Mol Biol. 2013 Nov;20(11):1310-7. doi: 10.1038/nsmb.2687. Epub 2013, Oct 20. PMID:24141706 doi:http://dx.doi.org/10.1038/nsmb.2687
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