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6uwf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==GltPh in complex with L-aspartate and sodium ions in outward-facing state== | |
| + | <StructureSection load='6uwf' size='340' side='right'caption='[[6uwf]], [[Resolution|resolution]] 3.08Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6uwf]] is a 1 chain structure with sequence from [https://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 [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=6uwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uwf OCA], [https://pdbe.org/6uwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uwf RCSB], [https://www.ebi.ac.uk/pdbsum/6uwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uwf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | Use of paramagnetic (19)F NMR to monitor domain movement in a glutamate transporter homolog.,Huang Y, Wang X, Lv G, Razavi AM, Huysmans GHM, Weinstein H, Bracken C, Eliezer D, Boudker O Nat Chem Biol. 2020 Sep;16(9):1006-1012. doi: 10.1038/s41589-020-0561-6. Epub, 2020 Jun 8. PMID:32514183<ref>PMID:32514183</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6uwf" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Symporter 3D structures|Symporter 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Pyrococcus shinkaii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boudker, O]] | ||
| + | [[Category: Wang, X]] | ||
| + | [[Category: Aspartate transporter]] | ||
| + | [[Category: Transport protein]] | ||
Current revision
GltPh in complex with L-aspartate and sodium ions in outward-facing state
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