› 7dys

Electron Microscopy
3.18Å resolution

CryoEM structure of full length mouse TRPML2

Released:
DOI: 10.2210/pdb7dys/pdb
PDB entry 7dys coloured by chain, front view.
PDB entry 7dys coloured by chain, side view.
PDB entry 7dys coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Cryo-EM structure of mouse TRPML2 in lipid nanodiscs.
Song X, Li J, Tian M, Zhu H, Hu X, Zhang Y, Cao Y, Ye H, McCormick PJ, Zeng B, Fu Y, Duan J, Zhang J
OpenAccess logo J Biol Chem 298 101487 (2022)
PMID: 34915027
Related structures: EMD-30924

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185095 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mucolipin-2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 518 amino acids
Theoretical weight: 60.01 KDa
Source organism: Mus musculus
Expression system: Mammalian expression vector HA-MCS-pcDNA3.1
UniProt:
  • Canonical: Q8K595 (Residues: 1-518; Coverage: 92%)
Gene name: Mcoln2
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.18Å
Relevant EMDB volumes: EMD-30924
Expression system: Mammalian expression vector HA-MCS-pcDNA3.1

Quick links

Citations

2 review citations

Mutation of TRPML1 Channel and Pathogenesis of Neurodegeneration in Haimeria.
Gao et al. (2023)
1 more

1 mention without citation

Cryo-EM structure of mouse TRPML2 in lipid nanodiscs.
Song et al. (2022)