8rg7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==BmrA E504-R6G-25uMATP-Mg== | |
| - | + | <StructureSection load='8rg7' size='340' side='right'caption='[[8rg7]], [[Resolution|resolution]] 3.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8rg7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RG7 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RHQ:RHODAMINE+6G'>RHQ</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8rg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rg7 OCA], [https://pdbe.org/8rg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rg7 RCSB], [https://www.ebi.ac.uk/pdbsum/8rg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rg7 ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: Gobet | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/BMRA_BACSU BMRA_BACSU] An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation (PubMed:18215075). Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).<ref>PMID:18215075</ref> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chaptal V]] | ||
| + | [[Category: Falson P]] | ||
| + | [[Category: Gobet A]] | ||
| + | [[Category: Schoehn G]] | ||
| + | [[Category: Zarkadas E]] | ||
Current revision
BmrA E504-R6G-25uMATP-Mg
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