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==Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC== | |||
<StructureSection load='3ppn' size='340' side='right' caption='[[3ppn]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ppn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPN FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ppo|3ppo]], [[3ppp|3ppp]], [[3ppq|3ppq]], [[3ppr|3ppr]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">opuCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ppn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppn RCSB], [http://www.ebi.ac.uk/pdbsum/3ppn PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[ABC transporter|ABC transporter]] | *[[ABC transporter|ABC transporter]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus globigii migula 1900]] | [[Category: Bacillus globigii migula 1900]] | ||
[[Category: Chen, Y | [[Category: Chen, Y]] | ||
[[Category: Du, Y | [[Category: Du, Y]] | ||
[[Category: He, Y X | [[Category: He, Y X]] | ||
[[Category: Shi, W W | [[Category: Shi, W W]] | ||
[[Category: Yang, Y H | [[Category: Yang, Y H]] | ||
[[Category: Zhou, C Z | [[Category: Zhou, C Z]] | ||
[[Category: Alpha-beta-alpha sandwich]] | [[Category: Alpha-beta-alpha sandwich]] | ||
[[Category: Compatible solute]] | [[Category: Compatible solute]] | ||
[[Category: Osmoprotectant]] | [[Category: Osmoprotectant]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 05:48, 25 December 2014
Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuCStructures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC
Structural highlights
Function[OPUCC_BACSU] Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.[1] [2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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