2ZFI: Crystal Structure Of The Kif1a Motor Domain Before Mg Release

Mg-ADP release is considered to be a crucial process for the regulation and motility of kinesin. To gain insight into the structural basis of this process, we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during and after Mg(2+) release. On the basis of new structural and mutagenesis data, we propose a model mechanism for microtubule activation of Mg-ADP release from KIF1A. In our model, a specific interaction between loop L7 of KIF1A and beta-tubulin reconfigures the KIF1A active site by shifting the relative positions of switches I and II. This leads to the sequential release of a group of water molecules that sits over the Mg(2+) in the active site, followed by Mg(2+) and finally the ADP. We further propose that this set of events is linked to a strain-dependent docking of the neck linker to the motor core, which produces a two-step power stroke.
PDB ID: 2ZFIDownload
MMDB ID: 66869
PDB Deposition Date: 2008/1/7
Updated in MMDB: 2017/09
Experimental Method:
x-ray diffraction
Resolution: 1.55  Å
Source Organism:
Similar Structures:
Biological Unit for 2ZFI: monomeric; determined by author and by software (PISA)
Molecular Components in 2ZFI
Label Count Molecule
Protein (1 molecule)
Kinesin-like Protein Kif1a, Kinesin Heavy Chain Isoform 5C
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB