4llh: Difference between revisions
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==Substrate bound outward-open state of the symporter BetP== | ==Substrate bound outward-open state of the symporter BetP== | ||
<StructureSection load='4llh' size='340' side='right' caption='[[4llh]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4llh' size='340' side='right' caption='[[4llh]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4llh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LLH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4llh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LLH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1Y8:2-(TRIMETHYL-LAMBDA~5~-ARSANYL)ETHANOL'>1Y8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CM5:5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE'>CM5</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1Y8:2-(TRIMETHYL-LAMBDA~5~-ARSANYL)ETHANOL'>1Y8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CM5:5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE'>CM5</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4llh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4llh RCSB], [http://www.ebi.ac.uk/pdbsum/4llh PDBsum]</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=4llh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llh OCA], [http://pdbe.org/4llh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4llh RCSB], [http://www.ebi.ac.uk/pdbsum/4llh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4llh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4llh" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:01, 5 August 2016
Substrate bound outward-open state of the symporter BetPSubstrate bound outward-open state of the symporter BetP
Structural highlights
Function[BETP_CORGL] High-affinity uptake of glycine betaine (By similarity). Publication Abstract from PubMedThe Na(+)-coupled betaine symporter BetP shares a highly conserved fold with other sequence unrelated secondary transporters, for example, with neurotransmitter symporters. Recently, we obtained atomic structures of BetP in distinct conformational states, which elucidated parts of its alternating-access mechanism. Here, we report a structure of BetP in a new outward-open state in complex with an anomalous scattering substrate, adding a fundamental piece to an unprecedented set of structural snapshots for a secondary transporter. In combination with molecular dynamics simulations these structural data highlight important features of the sequential formation of the substrate and sodium-binding sites, in which coordinating water molecules play a crucial role. We observe a strictly interdependent binding of betaine and sodium ions during the coupling process. All three sites undergo progressive reshaping and dehydration during the alternating-access cycle, with the most optimal coordination of all substrates found in the closed state. Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na(+) coupling.,Perez C, Faust B, Mehdipour AR, Francesconi KA, Forrest LR, Ziegler C Nat Commun. 2014 Jul 15;5:4231. doi: 10.1038/ncomms5231. PMID:25023443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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