4wit: Difference between revisions
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New page: '''Unreleased structure''' The entry 4wit is ON HOLD Authors: Dutzler, R., Brunner, J.D., Lim, N.K., Schenck, S. Description: TMEM16 lipid scramblase in crystal form 2 |
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The | ==TMEM16 lipid scramblase in crystal form 2== | ||
<StructureSection load='4wit' size='340' side='right'caption='[[4wit]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_vanettenii_77-13-4 Fusarium vanettenii 77-13-4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WIT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wit OCA], [https://pdbe.org/4wit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wit RCSB], [https://www.ebi.ac.uk/pdbsum/4wit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wit ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C7Z7K1_FUSV7 C7Z7K1_FUSV7] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional diversity. This family contains the long sought-after Ca2+-activated chloride channels as well as lipid scramblases and cation channels. Here we present the crystal structure of a TMEM16 family member from the fungus Nectria haematococca that operates as a Ca2+-activated lipid scramblase. Each subunit of the homodimeric protein contains ten transmembrane helices and a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca2+-binding site located within the hydrophobic core of the membrane. Mutations of residues involved in Ca2+ coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl- channel TMEM16A. The structure reveals the general architecture of the family and its mode of Ca2+ activation. It also provides insight into potential scrambling mechanisms and serves as a framework to unravel the conduction of ions in certain TMEM16 proteins. | |||
X-ray structure of a calcium-activated TMEM16 lipid scramblase.,Brunner JD, Lim NK, Schenck S, Duerst A, Dutzler R Nature. 2014 Nov 12. doi: 10.1038/nature13984. PMID:25383531<ref>PMID:25383531</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4wit" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Anoctamin 3D structures|Anoctamin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fusarium vanettenii 77-13-4]] | |||
[[Category: Large Structures]] | |||
[[Category: Brunner JD]] | |||
[[Category: Dutzler R]] | |||
[[Category: Lim NK]] | |||
[[Category: Schenck S]] | |||
Latest revision as of 11:27, 9 May 2024
TMEM16 lipid scramblase in crystal form 2
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