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Structure paper

TitleThe structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 3956, Year 2019
Publish dateSep 2, 2019
AuthorsSimon R Bushell / Ashley C W Pike / Maria E Falzone / Nils J G Rorsman / Chau M Ta / Robin A Corey / Thomas D Newport / John C Christianson / Lara F Scofano / Chitra A Shintre / Annamaria Tessitore / Amy Chu / Qinrui Wang / Leela Shrestha / Shubhashish M M Mukhopadhyay / James D Love / Nicola A Burgess-Brown / Rebecca Sitsapesan / Phillip J Stansfeld / Juha T Huiskonen / Paolo Tammaro / Alessio Accardi / Elisabeth P Carpenter /
PubMed AbstractMembranes in cells have defined distributions of lipids in each leaflet, controlled by lipid scramblases and flip/floppases. However, for some intracellular membranes such as the endoplasmic ...Membranes in cells have defined distributions of lipids in each leaflet, controlled by lipid scramblases and flip/floppases. However, for some intracellular membranes such as the endoplasmic reticulum (ER) the scramblases have not been identified. Members of the TMEM16 family have either lipid scramblase or chloride channel activity. Although TMEM16K is widely distributed and associated with the neurological disorder autosomal recessive spinocerebellar ataxia type 10 (SCAR10), its location in cells, function and structure are largely uncharacterised. Here we show that TMEM16K is an ER-resident lipid scramblase with a requirement for short chain lipids and calcium for robust activity. Crystal structures of TMEM16K show a scramblase fold, with an open lipid transporting groove. Additional cryo-EM structures reveal extensive conformational changes from the cytoplasmic to the ER side of the membrane, giving a state with a closed lipid permeation pathway. Molecular dynamics simulations showed that the open-groove conformation is necessary for scramblase activity.
External linksNat Commun / PubMed:31477691 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.2 - 5.14 Å
Structure data

4746

6r7x

EMDB-4746, PDB-6r7x:
CryoEM structure of calcium-bound human TMEM16K / Anoctamin 10 in detergent (2mM Ca2+, closed form)
Method: EM (single particle) / Resolution: 3.47 Å

4747

6r7y

EMDB-4747, PDB-6r7y:
CryoEM structure of calcium-bound human TMEM16K / Anoctamin 10 in detergent (low Ca2+, closed form)
Method: EM (single particle) / Resolution: 4.2 Å

4748

6r7z

EMDB-4748, PDB-6r7z:
CryoEM structure of calcium-free human TMEM16K / Anoctamin 10 in detergent (closed form)
Method: EM (single particle) / Resolution: 5.14 Å

PDB-5oc9:
Crystal Structure of human TMEM16K / Anoctamin 10
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-6r65:
Crystal Structure of human TMEM16K / Anoctamin 10 (Form 2)
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-79M:
(2R)-2,3-dihydroxypropyl (7Z)-hexadec-7-enoate

ChemComp-HOH:
WATER / Water

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

ChemComp-UMQ:
UNDECYL-MALTOSIDE / detergent*YM

Source
  • homo sapiens (human)
KeywordsLIPID TRANSPORT / MEMBRANE PROTEIN / CALCIUM ACTIVATION / TRANSPORT PROTEIN / Structural Genomics / Structural Genomics Consortium / SGC

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