4llh: Difference between revisions
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<tr><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><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> | ||
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== Publication Abstract from PubMed == | |||
The 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<ref>PMID:25023443</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:31, 30 July 2014
Substrate bound outward-open state of the symporter BetPSubstrate bound outward-open state of the symporter BetP
Structural highlights
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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