› 6rzb

Electron Microscopy
5Å resolution

Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to microtubules

Released:
DOI: 10.2210/pdb6rzb/pdb
PDB 6rzb coloured by chain and viewed from the front.
PDB 6rzb coloured by chain and viewed from the side.
PDB 6rzb coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.
Lacey SE, He S, Scheres SH, Carter AP
OpenAccess logo Elife 8 (2019)
PMID: 31264960
Related structures: EMD-10061

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Tubulin alpha-1B chain Chain: A
Molecule details ›
Chain: A
Length: 437 amino acids
Theoretical weight: 48.68 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: Q2XVP4 (Residues: 1-437; Coverage: 97%)
Gene name: TUBA1B
Sequence domains:
Tubulin beta chain Chain: B
Molecule details ›
Chain: B
Length: 426 amino acids
Theoretical weight: 47.83 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P02554 (Residues: 1-426; Coverage: 96%)
Sequence domains:
Cytoplasmic dynein 1 heavy chain 1 Chain: C
Molecule details ›
Chain: C
Length: 149 amino acids
Theoretical weight: 16.89 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JHU4 (Residues: 3270-3418; Coverage: 3%)
Gene names: Dhc1, Dnch1, Dnchc1, Dyhc, Dync1h1

Ligands and Environments

4 bound ligands:
Ligand GTP 1 x GTP
Ligand MG 1 x MG
Ligand GDP 1 x GDP
Ligand TA1 1 x TA1
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 5Å
Relevant EMDB volumes: EMD-10061
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Tubulin lattice in cilia is in a stressed form regulated by microtubule inner proteins.
Ichikawa et al. (2019)