4wis: Difference between revisions

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-'''Unreleased structure'''
-The entry 4wis is ON HOLD
+==Crystal structure of the lipid scramblase nhTMEM16 in crystal form 1==
+<StructureSection load='4wis' size='340' side='right'caption='[[4wis]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wis]] 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=4WIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WIS 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]] 3.3&#8491;</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=4wis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wis OCA], [https://pdbe.org/4wis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wis RCSB], [https://www.ebi.ac.uk/pdbsum/4wis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wis 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.
-Authors: Dutzler, R., Brunner, J.D., Lim, N.K., Schenck, S.
+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>
-Description: Crystal structure of the lipid scramblase nhTMEM16 in crystal form 1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4wis" 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]]