› 1f9t

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURES OF KINESIN MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE MOTOR ATPASE

Released:
DOI: 10.2210/pdb1f9t/pdb
PDB entry 1f9t coloured by chain, front view.
PDB entry 1f9t coloured by chain, side view.
PDB entry 1f9t coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A structural pathway for activation of the kinesin motor ATPase.
Yun M, Zhang X, Park CG, Park HW, Endow SA
EMBO J 20 2611-8 (2001)
PMID: 11387196

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + a kinesin associated with a microtubule at position (n) = ADP + phosphate + a kinesin associated with a microtubule at position (n-1, toward the minus end)
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-147871 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinesin-like protein KAR3 Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 40.36 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P17119 (Residues: 372-729; Coverage: 49%)
Gene names: KAR3, P9659.16, YPR141C
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: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 43.61Å b: 78.81Å c: 47.17Å
α: 90° β: 105.01° γ: 90°
R-values:
R R work R free
0.213 0.213 0.244
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Molecular motors.
Schliwa et al. (2003)
8 more

8 mentions without citation

High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation.
Shang et al. (2014)
7 more