View source for 3ppq


==Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC==
<StructureSection load='3ppq' size='340' side='right'caption='[[3ppq]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ppq]] 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=3PPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPQ 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]] 1.91&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</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=3ppq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppq OCA], [https://pdbe.org/3ppq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppq RCSB], [https://www.ebi.ac.uk/pdbsum/3ppq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OPUCC_BACSU OPUCC_BACSU] Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.<ref>PMID:10216873</ref> <ref>PMID:8752321</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The compatible solute ATP-binding cassette (ABC) transporters are indispensable for acquiring a variety of compatible solutes under osmotic stress in Bacillus subtilis. The substrate-binding protein OpuCC of the ABC transporter OpuC can recognize a broad spectrum of compatible solutes, compared to its 70% sequence-identical paralog OpuBC that can solely bind choline. To explore the structural basis of this difference of substrate specificity, we determined crystal structures of OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with substrate-binding pocket located at the inter-domain cleft. Upon substrate-binding, the two domains shift towards each other to trap the substrate. Comparative structural analysis revealed a plastic pocket that fits various compatible solutes, which attributes the multiple-substrate binding property to OpuCC. This plasticity is a gain-of-function via a single-residue mutation of Thr94 in OpuCC versus Asp96 in OpuBC.

Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC.,Du Y, Shi WW, He YX, Yang YH, Zhou CZ, Chen Y Biochem J. 2011 Mar 3. PMID:21366542<ref>PMID:21366542</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ppq" style="background-color:#fffaf0;"></div>

==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Chen Y]]
[[Category: Du Y]]
[[Category: He YX]]
[[Category: Shi WW]]
[[Category: Yang YH]]
[[Category: Zhou CZ]]