8ri1

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m (Protected "8ri1" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 8ri1 is ON HOLD until Paper Publication
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==BmrA E504-100uMATPMg==
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<StructureSection load='8ri1' size='340' side='right'caption='[[8ri1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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Authors: Gobet, A., Zarkadas, E., Schoehn, G., Falson, P., Chaptal, V.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ri1]] 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=8RI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RI1 FirstGlance]. <br>
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Description: BmrA E504-100uMATPMg
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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[[Category: Zarkadas, E]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ri1 OCA], [https://pdbe.org/8ri1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ri1 RCSB], [https://www.ebi.ac.uk/pdbsum/8ri1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ri1 ProSAT]</span></td></tr>
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[[Category: Schoehn, G]]
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</table>
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[[Category: Gobet, A]]
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== Function ==
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[[Category: Chaptal, V]]
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[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>
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[[Category: Falson, P]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus subtilis]]
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[[Category: Large Structures]]
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[[Category: Chaptal V]]
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[[Category: Falson P]]
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[[Category: Gobet A]]
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[[Category: Schoehn G]]
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[[Category: Zarkadas E]]

Current revision

BmrA E504-100uMATPMg

PDB ID 8ri1

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