6uwf

==GltPh in complex with L-aspartate and sodium ions in outward-facing state==

<StructureSection load='6uwf' size='340' side='right'caption='[[6uwf]], [[Resolution|resolution]] 3.08&Aring;' scene=''>

<table><tr><td colspan='2'>[[6uwf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UWF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UWF FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6uwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uwf OCA], [http://pdbe.org/6uwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uwf RCSB], [http://www.ebi.ac.uk/pdbsum/6uwf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uwf ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

In proteins where conformational changes are functionally important, the number of accessible states and their dynamics are often difficult to establish. Here we describe a novel (19)F-NMR spectroscopy approach to probe dynamics of large membrane proteins. We labeled a glutamate transporter homolog with a (19)F probe via cysteine chemistry and with a Ni(2+) ion via chelation by a di-histidine motif. We used distance-dependent enhancement of the longitudinal relaxation of (19)F nuclei by the paramagnetic metal to assign the observed resonances. We identified one inward- and two outward-facing states of the transporter, in which the substrate-binding site is near the extracellular and intracellular solutions, respectively. We then resolved the structure of the unanticipated second outward-facing state by cryo-EM. Finally, we showed that the rates of the conformational exchange are accessible from measurements of the metal-enhanced longitudinal relaxation of (19)F nuclei.

 

== References ==

[[Category: Pyrococcus shinkaii]]

[[Category: Boudker, O]]

[[Category: Transport protein]]