› 1v8j

X-ray diffraction
3.24Å resolution

The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-ADP

Released:
DOI: 10.2210/pdb1v8j/pdb
PDB entry 1v8j coloured by chain, front view.
PDB entry 1v8j coloured by chain, side view.
PDB entry 1v8j coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops.
Ogawa T, Nitta R, Okada Y, Hirokawa N
Cell 116 591-602 (2004)
PMID: 14980225

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinesin-like protein KIF2C Chain: A
Molecule details ›
Chain: A
Length: 410 amino acids
Theoretical weight: 46.8 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q922S8 (Residues: 183-585; Coverage: 56%)
Gene name: Kif2c
Sequence domains: Kinesin motor domain
Structure domains: Kinesin motor domain

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C222
Unit cell:
a: 61.209Å b: 192.453Å c: 73.554Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.248 0.291
Expression system: Escherichia coli

Quick links

Citations

33 review citations

Molecular motors and mechanisms of directional transport in neurons.
Hirokawa et al. (2005)
32 more

7 mentions without citation

Electrostatically biased binding of kinesin to microtubules.
Grant et al. (2011)
6 more