› 5mw1

Electron Microscopy
3.8Å resolution

cryoEM structure of crenactin double helical filament at 3.8A resolution

Released:
DOI: 10.2210/pdb5mw1/pdb
PDB entry 5mw1 coloured by chain, front view.
PDB entry 5mw1 coloured by chain, side view.
PDB entry 5mw1 coloured by chain, top view.
Source organism: Pyrobaculum calidifontis
Primary publication:
Crenactin forms actin-like double helical filaments regulated by arcadin-2.
Izoré T, Kureisaite-Ciziene D, McLaughlin SH, Löwe J
Elife 5 (2016)
PMID: 27852434
Related structures: EMD-4117

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Crenactin Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 432 amino acids
Theoretical weight: 48.43 KDa
Source organism: Pyrobaculum calidifontis
Expression system: Escherichia coli
UniProt:
  • Canonical: A3MWN5 (Residues: 1-432; Coverage: 100%)
Gene names: Pcal_1635, cren-1
Sequence domains: Actin
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 6 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-4117
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Dividing the Archaeal Way: The Ancient Cdv Cell-Division Machinery.
Caspi et al. (2018)
7 more

2 mentions without citation

Suramin and NF449 are IP5K inhibitors that disrupt inositol hexakisphosphate-mediated regulation of cullin-RING ligase and sensitize cancer cells to MLN4924/pevonedistat.
Zhang et al. (2020)
1 more