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Structure paper

TitleCryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail.
Journal, issue, pagesSci Adv, Vol. 6, Issue 33, Page eabb0147, Year 2020
Publish dateAug 12, 2020
AuthorsYuxia Zhang / Michio Inoue / Akihisa Tsutsumi / Satoshi Watanabe / Tomohiro Nishizawa / Kazuhiro Nagata / Masahide Kikkawa / Kenji Inaba /
PubMed AbstractSarco/endoplasmic reticulum Ca ATPase (SERCA) pumps Ca from the cytosol into the ER and maintains the cellular calcium homeostasis. Herein, we present cryo-electron microscopy (cryo-EM) structures of ...Sarco/endoplasmic reticulum Ca ATPase (SERCA) pumps Ca from the cytosol into the ER and maintains the cellular calcium homeostasis. Herein, we present cryo-electron microscopy (cryo-EM) structures of human SERCA2b in E1∙2Ca-adenylyl methylenediphosphonate (AMPPCP) and E2-BeF states at 2.9- and 2.8-Å resolutions, respectively. The structures revealed that the luminal extension tail (LE) characteristic of SERCA2b runs parallel to the lipid-water boundary near the luminal ends of transmembrane (TM) helices TM10 and TM7 and approaches the luminal loop flanked by TM7 and TM8. While the LE served to stabilize the cytosolic and TM domain arrangement of SERCA2b, deletion of the LE rendered the overall conformation resemble that of SERCA1a and SERCA2a and allowed multiple conformations. Thus, the LE appears to play a critical role in conformational regulation in SERCA2b, which likely explains the different kinetic properties of SERCA2b from those of other isoforms lacking the LE.
External linksSci Adv / PubMed:32851169 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.4 Å
Structure data

0912

6lle

EMDB-0912: WT transporter state2
PDB-6lle: CryoEM structure of SERCA2b WT in E1-2Ca2+-AMPPCP state.
Method: EM (single particle) / Resolution: 2.9 Å

0915

6lly

EMDB-0915: WT transporter state1
PDB-6lly: CryoEM structure of SERCA2b WT in E2-BeF3- state
Method: EM (single particle) / Resolution: 2.8 Å

0924

6ln5

EMDB-0924, PDB-6ln5:
CryoEM structure of SERCA2b T1032stop in E1-2Ca2+-AMPPCP (class1)
Method: EM (single particle) / Resolution: 2.8 Å

0925

6ln6

EMDB-0925, PDB-6ln6:
CryoEM structure of SERCA2b T1032stop in E1-2Ca2+-AMPPCP (class2)
Method: EM (single particle) / Resolution: 2.9 Å

0926

6ln7

EMDB-0926: mutation transporter state2-3
PDB-6ln7: CryoEM structure of SERCA2b T1032stop in E1-2Ca2+-AMPPCP (class3)
Method: EM (single particle) / Resolution: 2.8 Å

0927

6ln8

EMDB-0927: mutation transporter state1-1
PDB-6ln8: CryoEM structure of SERCA2b T1032stop in E2-BeF3- state (class1)
Method: EM (single particle) / Resolution: 3.1 Å

0928

6ln9

EMDB-0928, PDB-6ln9:
CryoEM structure of SERCA2b T1032stop in E2-BeF3- state (class2)
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

Source
  • homo sapiens (human)
KeywordsMETAL TRANSPORT / calcium / cacium

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