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Structure paper

TitleModulation of cardiac ryanodine receptor 2 by calmodulin.
Journal, issue, pagesNature, Vol. 572, Issue 7769, Page 347-351, Year 2019
Publish dateJul 5, 2019
AuthorsDeshun Gong / Ximin Chi / Jinhong Wei / Gewei Zhou / Gaoxingyu Huang / Lin Zhang / Ruiwu Wang / Jianlin Lei / S R Wayne Chen / Nieng Yan /
PubMed AbstractThe high-conductance intracellular calcium (Ca) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 ...The high-conductance intracellular calcium (Ca) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca-dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca-CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca binding to CaM, rather than to RyR2. Ca-CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca-activated channel. By contrast, the pore of the ATP, caffeine and Ca-activated channel remains open in the presence of Ca-CaM, which suggests that Ca-CaM is one of the many competing modulators of RyR2 gating.
External linksNature / PubMed:31278385
MethodsEM (single particle)
Resolution3.6 - 4.4 Å
Structure data

9831

6ji0

EMDB-9831, PDB-6ji0:
Structure of RyR2 (F/A/C/Ca2+ dataset)
Method: EM (single particle) / Resolution: 4.2 Å

9833

6ji8

EMDB-9833, PDB-6ji8:
Structure of RyR2 (F/apoCaM dataset)
Method: EM (single particle) / Resolution: 3.6 Å

9834

6jii

EMDB-9834, PDB-6jii:
Structure of RyR2 (F/A/C/L-Ca2+/apo-CaM-M dataset)
Method: EM (single particle) / Resolution: 4.2 Å

9836

6jiu

EMDB-9836, PDB-6jiu:
Structure of RyR2 (F/A/C/L-Ca2+/Ca2+CaM dataset)
Method: EM (single particle) / Resolution: 4.2 Å

9837

6jiy

EMDB-9837, PDB-6jiy:
Structure of RyR2 (F/A/C/H-Ca2+/Ca2+CaM dataset)
Method: EM (single particle) / Resolution: 3.9 Å

9879

6jrr

EMDB-9879, PDB-6jrr:
Structure of RyR2 (*F/A/C/L-Ca2+ dataset)
Method: EM (single particle) / Resolution: 3.9 Å

9880

6jrs

EMDB-9880, PDB-6jrs:
Structure of RyR2 (*F/A/C/L-Ca2+/Ca2+-CaM dataset)
Method: EM (single particle) / Resolution: 3.7 Å

9889

6jv2

EMDB-9889, PDB-6jv2:
Structure of RyR2 (P/L-Ca2+/Ca2+-CaM dataset)
Method: EM (single particle) / Resolution: 4.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-CA:
Unknown entry

ChemComp-CFF:
CAFFEINE / medication*YM / Caffeine (data page)

Source
  • sus scrofa (pig)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / cryo-EM / MEMBRANE PROTEIN/ISOMERASE / MEMBRANE PROTEIN-ISOMERASE complex

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