2HXH

KIF1A head-microtubule complex structure in adp-form

Summary for 2HXH

• Entry DOI: 10.2210/pdb2hxh/pdb
• Related: 1I5S 1IA0 1JFF 2HXF
• Descriptor: Tubulin alpha chain, Tubulin beta chain, Kinesin-like protein KIF1A, ... (8 entities in total)
• Functional Keywords: microtubule-based motor, transport protein
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 146627.99

Authors

Kikkawa, M.,Hirokawa, N. (deposition date: 2006-08-03, release date: 2006-10-10, Last modification date: 2024-06-05)

Primary citation

Kikkawa, M.,Hirokawa, N.
High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
Embo J., 25:4187-4194, 2006

PubMed Abstract: Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor.

PubMed: 16946706
DOI: 10.1038/sj.emboj.7601299

Experimental method

ELECTRON MICROSCOPY (11 Å)