Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into the regulation of RyR1 by S100A1.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 121, Issue 27, Page e2400497121, Year 2024
Publish date	Jul 2, 2024
Authors	Gunnar Weninger / Marco C Miotto / Carl Tchagou / Steven Reiken / Haikel Dridi / Sören Brandenburg / Gabriel C Riedemann / Qi Yuan / Yang Liu / Alexander Chang / Anetta Wronska / Stephan E Lehnart / Andrew R Marks /
PubMed Abstract	S100A1, a small homodimeric EF-hand Ca-binding protein (~21 kDa), plays an important regulatory role in Ca signaling pathways involved in various biological functions including Ca cycling and ...S100A1, a small homodimeric EF-hand Ca-binding protein (~21 kDa), plays an important regulatory role in Ca signaling pathways involved in various biological functions including Ca cycling and contractile performance in skeletal and cardiac myocytes. One key target of the S100A1 interactome is the ryanodine receptor (RyR), a huge homotetrameric Ca release channel (~2.3 MDa) of the sarcoplasmic reticulum. Here, we report cryoelectron microscopy structures of S100A1 bound to RyR1, the skeletal muscle isoform, in absence and presence of Ca. Ca-free apo-S100A1 binds beneath the bridging solenoid (BSol) and forms contacts with the junctional solenoid and the shell-core linker of RyR1. Upon Ca-binding, S100A1 undergoes a conformational change resulting in the exposure of the hydrophobic pocket known to serve as a major interaction site of S100A1. Through interactions of the hydrophobic pocket with RyR1, Ca-bound S100A1 intrudes deeper into the RyR1 structure beneath BSol than the apo-form and induces sideways motions of the C-terminal BSol region toward the adjacent RyR1 protomer resulting in tighter interprotomer contacts. Interestingly, the second hydrophobic pocket of the S100A1-dimer is largely exposed at the hydrophilic surface making it prone to interactions with the local environment, suggesting that S100A1 could be involved in forming larger heterocomplexes of RyRs with other protein partners. Since S100A1 interactions stabilizing BSol are implicated in the regulation of RyR-mediated Ca release, the characterization of the S100A1 binding site conserved between RyR isoforms may provide the structural basis for the development of therapeutic strategies regarding treatments of RyR-related disorders.
External links	Proc Natl Acad Sci U S A / PubMed:38917010 / PubMed Central
Methods	EM (single particle)
Resolution	2.29 - 3.78 Å
Structure data	43283 8vjj EMDB-43283, PDB-8vjj: Structure of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.53 Å 43284 8vjk EMDB-43284, PDB-8vjk: Structure of mouse RyR1 (high-Ca2+/CFF/ATP dataset) Method: EM (single particle) / Resolution: 2.92 Å EMDB-43295: Raw consensus map of mouse RyR1 in complex with S100A1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 3.21 Å EMDB-43296: Constituent EM map: Focused refinement S100A1 of mouse RyR1 in complex with S100A1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 3.51 Å EMDB-43297: Constituent EM map: Focused refinement BSol+S100A1 of mouse RyR1 in complex with S100A1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 3.19 Å EMDB-43298: Constituent EM map: Focused refinement JSol+CSol+S100A1 of mouse RyR1 in complex with S100A1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.97 Å 43299 8vk3 EMDB-43299, PDB-8vk3: Structure of mouse RyR1 in complex with S100A1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 3.21 Å EMDB-43300: Raw consensus map of mouse RyR1 in complex with S100A1 (high-Ca2+/CFF/ATP dataset) Method: EM (single particle) / Resolution: 3.56 Å EMDB-43301: Constituent EM map: Focused refinement JSol+CSol+S100A1 of mouse RyR1 in complex with S100A1 (high-Ca2+/CFF/ATP dataset) Method: EM (single particle) / Resolution: 3.29 Å EMDB-43302: Constituent EM map: Focused refinement BSol+S100A1 of mouse RyR1 in complex with S100A1 (high-Ca2+/CFF/ATP dataset) Method: EM (single particle) / Resolution: 3.78 Å EMDB-43303: Constituent EM map: Focused refinement S100A1 of mouse RyR1 in complex with S100A1 (high-Ca2+/CFF/ATP dataset) Method: EM (single particle) / Resolution: 3.76 Å 43304 8vk4 EMDB-43304, PDB-8vk4: Structure of mouse RyR1 in complex with S100A1 (high-Ca2+/CFF/ATP dataset) Method: EM (single particle) / Resolution: 3.56 Å EMDB-43307: Raw consensus map of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.53 Å EMDB-43308: Constituent EM map: Focused refinement NTD+SPRY+Calstabin-1 of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.29 Å EMDB-43309: Constituent EM map: Focused refinement JSol+CSol of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.31 Å EMDB-43310: Constituent EM map: Focused refinement BSol of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.46 Å EMDB-43311: Constituent EM map: Focused refinement TaF+TM+CTD of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.35 Å EMDB-43312: Constituent EM map: Focused refinement Ry1&2 of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.46 Å EMDB-43313: Constituent EM map: Focused refinement Ry3&4 of mouse RyR1 (EGTA-only dataset) Method: EM (single particle) / Resolution: 2.55 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-PCW: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipidYM ChemComp-CFF: CAFFEINE / medicationYM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-CA*: Unknown entry
Source	mus musculus (house mouse)
Keywords	MEMBRANE PROTEIN / Calcium / Ion Channel