6uwl: Difference between revisions

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<StructureSection load='6uwl' size='340' side='right'caption='[[6uwl]], [[Resolution|resolution]] 3.62&Aring;' scene=''>
<StructureSection load='6uwl' size='340' side='right'caption='[[6uwl]], [[Resolution|resolution]] 3.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6uwl]] 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=6UWL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UWL FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UWL 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.62&#8491;</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='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>, <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=6uwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uwl OCA], [http://pdbe.org/6uwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uwl RCSB], [http://www.ebi.ac.uk/pdbsum/6uwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uwl ProSAT]</span></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=6uwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uwl OCA], [https://pdbe.org/6uwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uwl RCSB], [https://www.ebi.ac.uk/pdbsum/6uwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uwl ProSAT]</span></td></tr>
</table>
</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>
==See Also==
 
*[[Symporter 3D structures|Symporter 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6uwl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrococcus shinkaii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boudker, O]]
[[Category: Boudker O]]
[[Category: Wang, X]]
[[Category: Wang X]]
[[Category: Aspartate transporter]]
[[Category: Transport protein]]

Latest revision as of 09:58, 25 December 2024

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

6uwl, resolution 3.62Å

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