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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== | | ==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]] 1.91Å' scene=''> | + | <StructureSection load='3ppq' size='340' side='right'caption='[[3ppq]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ppq]] 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=3PPQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPQ FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ppn|3ppn]], [[3ppo|3ppo]], [[3ppp|3ppp]], [[3ppr|3ppr]]</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='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'>[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> |
| - | <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=3ppq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppq OCA], [http://pdbe.org/3ppq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ppq RCSB], [http://www.ebi.ac.uk/pdbsum/3ppq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[ABC transporter|ABC transporter]] | + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Chen, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Du, Y]] | + | [[Category: Chen Y]] |
| - | [[Category: He, Y X]] | + | [[Category: Du Y]] |
| - | [[Category: Shi, W W]] | + | [[Category: He YX]] |
| - | [[Category: Yang, Y H]] | + | [[Category: Shi WW]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Yang YH]] |
| - | [[Category: Alpha-beta-alpha sandwich]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Osmoprotectant]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| 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 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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kappes RM, Kempf B, Kneip S, Boch J, Gade J, Meier-Wagner J, Bremer E. Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Mol Microbiol. 1999 Apr;32(1):203-16. PMID:10216873
- ↑ Kappes RM, Kempf B, Bremer E. Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD. J Bacteriol. 1996 Sep;178(17):5071-9. PMID:8752321
- ↑ Du Y, Shi WW, He YX, Yang YH, Zhou CZ, Chen Y. Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC. Biochem J. 2011 Mar 3. PMID:21366542 doi:10.1042/BJ20102097
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