4llh: Difference between revisions

<StructureSection load='4llh' size='340' side='right' caption='[[4llh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<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>

<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>

[[http://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL]] High-affinity uptake of glycine betaine (By similarity).

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.

 

== References ==

[[Category: Faust, B]]

[[Category: Perez, C]]

[[Category: Ziegler, C]]

[[Category: Secondary transporter]]

[[Category: Transport protein]]