View source for 6yir


==Crystal structure of Bacillus subtilis MsmX ATPase==
<StructureSection load='6yir' size='340' side='right'caption='[[6yir]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yir]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YIR 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]] 1.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6yir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yir OCA], [https://pdbe.org/6yir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yir RCSB], [https://www.ebi.ac.uk/pdbsum/6yir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yir ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSMX_BACSU MSMX_BACSU] Part of the ABC transporter complex involved in maltodextrin import (Probable). Is also part of the ABC transporter complex MelEDC-MsmX involved in melibiose, raffinose and stachyose import (PubMed:31138628). Probably responsible for energy coupling to the transport system (Probable).<ref>PMID:31138628</ref> <ref>PMID:16707683</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP-binding cassette (ABC) type I importers are widespread in bacteria and play a crucial role in its survival and pathogenesis. They share the same modular architecture comprising two intracellular nucleotide-binding domains (NBDs), two transmembrane domains (TMDs) and a substrate-binding protein. The NBDs bind and hydrolyze ATP, thereby generating conformational changes that are coupled to the TMDs and lead to substrate translocation. A group of multitask NBDs that are able to serve as the cellular motor for multiple sugar importers was recently discovered. To understand why some ABC importers share energy-coupling components, we used the MsmX ATPase from Bacillus subtilis as a model for biological and structural studies. Here we report the first examples of functional hybrid interspecies ABC type I importers in which the NBDs could be exchanged. Furthermore, the first crystal structure of an assigned multitask NBD provides a framework to understand the molecular basis of the broader specificity of interaction with the TMDs.

Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.,Leisico F, Godinho LM, Goncalves IC, Silva SP, Carneiro B, Romao MJ, Santos-Silva T, de Sa-Nogueira I Sci Rep. 2020 Nov 11;10(1):19564. doi: 10.1038/s41598-020-76444-0. PMID:33177617<ref>PMID:33177617</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yir" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Leisico F]]
[[Category: Romao MJ]]
[[Category: Santos-Silva T]]