View source for 4wit

==TMEM16 lipid scramblase in crystal form 2==
<StructureSection load='4wit' size='340' side='right' caption='[[4wit]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wit]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wis|4wis]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wit OCA], [http://pdbe.org/4wit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wit RCSB], [http://www.ebi.ac.uk/pdbsum/4wit PDBsum]</span></td></tr>
</table>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4wit" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Brunner, J D]]
[[Category: Dutzler, R]]
[[Category: Lim, N K]]
[[Category: Schenck, S]]
[[Category: Calcium activation]]
[[Category: Lipid transport]]
[[Category: Membrane protein]]
[[Category: Transport protein]]