› 5ye5

Electron Microscopy
5.8Å resolution

structure of endo-lysosomal TRPML1 channel inserting into nanodisc

Released:
DOI: 10.2210/pdb5ye5/pdb
PDB entry 5ye5 coloured by chain, front view.
PDB entry 5ye5 coloured by chain, side view.
PDB entry 5ye5 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Cryo-EM structures of the mammalian endo-lysosomal TRPML1 channel elucidate the combined regulation mechanism.
Zhang S, Li N, Zeng W, Gao N, Yang M
Protein Cell 8 834-847 (2017)
PMID: 28936784
Related structures: EMD-6826

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-189325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mucolipin-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 580 amino acids
Theoretical weight: 65.57 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q99J21 (Residues: 1-580; Coverage: 100%)
Gene names: Mcoln1, Trpml1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand NAG 8 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 5.8Å
Relevant EMDB volumes: EMD-6826
Expression system: Homo sapiens

Quick links

Citations

11 review citations

Dawning of a new era in TRP channel structural biology by cryo-electron microscopy.
Madej et al. (2018)
10 more

2 mentions without citation

Cryo-EM structures of the mammalian endo-lysosomal TRPML1 channel elucidate the combined regulation mechanism.
Zhang et al. (2017)
1 more