8ri1: Difference between revisions

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'''Unreleased structure'''


The entry 8ri1 is ON HOLD  until Paper Publication
==BmrA E504-100uMATPMg==
 
<StructureSection load='8ri1' size='340' side='right'caption='[[8ri1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
Authors: Gobet, A., Zarkadas, E., Schoehn, G., Falson, P., Chaptal, V.
== Structural highlights ==
 
<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>
Description: BmrA E504-100uMATPMg
</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>
[[Category: Unreleased Structures]]
<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>
[[Category: Zarkadas, E]]
<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>
[[Category: Chaptal, V]]
</table>
[[Category: Schoehn, G]]
== Function ==
[[Category: Falson, P]]
[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: Gobet, A]]
== 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]]

Latest revision as of 06:15, 29 January 2025

BmrA E504-100uMATPMg

8ri1, resolution 3.60Å

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