4wit

TMEM16 lipid scramblase in crystal form 2TMEM16 lipid scramblase in crystal form 2

Structural highlights 4wit is a 2 chain structure with sequence from Fusarium vanettenii 77-13-4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C7Z7K1_FUSV7 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Anoctamin 3D structures

spinqualitylabelsall models 4wit, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image