|Entry||Database: PDB / ID: 6dmw|
|Title||Calmodulin-bound full-length rbTRPV5|
|Keywords||TRANSPORT PROTEIN / calmodulin / TRPV5 / full-length / calcium channel|
|Function / homology||EF-hand calcium-binding domain. / Transient receptor potential cation channel subfamily V / Ankyrin repeat profile. / EF-hand domain / Ankyrin repeat / Ion transport domain / Transient receptor potential cation channel subfamily V member 5/6 / Transient receptor potential cation channel subfamily V member 5 / EF-hand domain pair / EF-Hand 1, calcium-binding site ...EF-hand calcium-binding domain. / Transient receptor potential cation channel subfamily V / Ankyrin repeat profile. / EF-hand domain / Ankyrin repeat / Ion transport domain / Transient receptor potential cation channel subfamily V member 5/6 / Transient receptor potential cation channel subfamily V member 5 / EF-hand domain pair / EF-Hand 1, calcium-binding site / Ankyrin repeat-containing domain / EF-hand calcium-binding domain profile. / in:ipr004729: / Ankyrin repeat-containing domain superfamily / EF-hand domain pair / Calmodulin / Ion transport protein / Ankyrin repeats (3 copies) / Ankyrin repeat region circular profile. / regulation of store-operated calcium channel activity / calcium ion import across plasma membrane / calcium ion homeostasis / calcium channel regulator activity / regulation of urine volume / establishment of protein localization to membrane / type 3 metabotropic glutamate receptor binding / establishment of protein localization to mitochondrial membrane / positive regulation by host of symbiont cAMP-mediated signal transduction / N-terminal myristoylation domain binding / regulation of synaptic vesicle endocytosis / regulation of high voltage-gated calcium channel activity / protein phosphatase activator activity / adenylate cyclase activator activity / positive regulation of ryanodine-sensitive calcium-release channel activity / positive regulation of cyclic-nucleotide phosphodiesterase activity / catalytic complex / activation of adenylate cyclase activity / adenylate cyclase binding / enzyme regulator activity / detection of calcium ion / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction / voltage-gated potassium channel complex / calcium channel activity / calcium channel inhibitor activity / nitric-oxide synthase binding / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / positive regulation of phosphoprotein phosphatase activity / calcium channel complex / calcium ion transmembrane transport / sarcomere / titin binding / regulation of ryanodine-sensitive calcium-release channel activity / calcium ion transport / response to amphetamine / regulation of heart rate / phosphatidylinositol 3-kinase binding / calcium-mediated signaling / positive regulation of DNA binding / spindle microtubule / regulation of cytokinesis / regulation of synaptic vesicle exocytosis / nitric-oxide synthase regulator activity / calcium-dependent protein binding / spindle pole / protein tetramerization / positive regulation of nitric-oxide synthase activity / growth cone / protein homotetramerization / disordered domain specific binding / G2/M transition of mitotic cell cycle / apical plasma membrane / protein N-terminus binding / ion channel binding / calmodulin binding / neuron projection / centrosome / myelin sheath / protein domain specific binding / protein kinase binding / calcium ion binding / integral component of plasma membrane / mitochondrion / nucleoplasm / plasma membrane / nucleus / metal ion binding / cytosol / cytoplasm / Calmodulin-1 / Transient receptor potential cation channel subfamily V member 5|
Function and homology information
|Specimen source||Oryctolagus cuniculus (rabbit)|
Rattus norvegicus (Norway rat)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 4.4 Å resolution|
|Authors||Hughes, T.E.T. / Pumroy, R.A. / Moiseenkova-Bell, V.Y.|
|Citation||Journal: Nat Commun / Year: 2018|
Title: Structural insights on TRPV5 gating by endogenous modulators.
Authors: Taylor E T Hughes / Ruth A Pumroy / Aysenur Torun Yazici / Marina A Kasimova / Edwin C Fluck / Kevin W Huynh / Amrita Samanta / Sudheer K Molugu / Z Hong Zhou / Vincenzo Carnevale / Tibor Rohacs / Vera Y Moiseenkova-Bell
SummaryFull reportAbout validation report
|Date||Deposition: Jun 5, 2018 / Release: Oct 24, 2018|
|Structure viewer||Molecule: |
Downloads & links
A: Transient receptor potential cation channel subfamily V member 5
B: Transient receptor potential cation channel subfamily V member 5
C: Transient receptor potential cation channel subfamily V member 5
D: Transient receptor potential cation channel subfamily V member 5
Mass: 82899.656 Da / Num. of mol.: 4 / Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: Trpv5, Ecac1 / Production host: Saccharomyces cerevisiae (baker's yeast) / References: UniProt: Q9XSM3
Mass: 16852.545 Da / Num. of mol.: 1 / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Calm1, Calm, Cam, Cam1, CaMI / Production host: Escherichia coli (E. coli) / References: UniProt: P0DP29
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Buffer solution||pH: 8.8|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Details: unspecified|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 1 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C1|
|3D reconstruction||Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 47484 / Symmetry type: POINT|
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