2wit: Difference between revisions
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<StructureSection load='2wit' size='340' side='right'caption='[[2wit]], [[Resolution|resolution]] 3.35Å' scene=''> | <StructureSection load='2wit' size='340' side='right'caption='[[2wit]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wit]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2wit]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w8a 2w8a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WIT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BET:TRIMETHYL+GLYCINE'>BET</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wit OCA], [https://pdbe.org/2wit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wit RCSB], [https://www.ebi.ac.uk/pdbsum/2wit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wit ProSAT]</span></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=2wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wit OCA], [https://pdbe.org/2wit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wit RCSB], [https://www.ebi.ac.uk/pdbsum/2wit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wit ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL] High-affinity uptake of glycine betaine (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Corynebacterium glutamicum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ott | [[Category: Ott V]] | ||
[[Category: Ressl | [[Category: Ressl S]] | ||
[[Category: | [[Category: Terwisscha Van Scheltinga AC]] | ||
[[Category: Vonrhein | [[Category: Vonrhein C]] | ||
[[Category: Ziegler | [[Category: Ziegler C]] | ||
Latest revision as of 11:46, 15 November 2023
CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATECRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE
Structural highlights
FunctionBETP_CORGL High-affinity uptake of glycine betaine (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOsmoregulated transporters sense intracellular osmotic pressure and respond to hyperosmotic stress by accumulation of osmolytes to restore normal hydration levels. Here we report the determination of the X-ray structure of a member of the family of betaine/choline/carnitine transporters, the Na(+)-coupled symporter BetP from Corynebacterium glutamicum, which is a highly effective osmoregulated uptake system for glycine betaine. Glycine betaine is bound in a tryptophan box occluded from both sides of the membrane with aromatic side chains lining the transport pathway. BetP has the same overall fold as three unrelated Na(+)-coupled symporters. Whereas these are crystallized in either the outward-facing or the inward-facing conformation, the BetP structure reveals a unique intermediate conformation in the Na(+)-coupled transport cycle. The trimeric architecture of BetP and the break in three-fold symmetry by the osmosensing C-terminal helices suggest a regulatory mechanism of Na(+)-coupled osmolyte transport to counteract osmotic stress. Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP.,Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, Ziegler C Nature. 2009 Mar 5;458(7234):47-52. PMID:19262666[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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