1VFW

Crystal Structure of the Kif1A Motor Domain Complexed With Mg-AMPPNP

Summary for 1VFW

• Entry DOI: 10.2210/pdb1vfw/pdb
• Related: 1VFV 1VFX 1VFZ
• Descriptor: PROTEIN (Fusion protein consisting of Kinesin-like protein KIF1A, Kinesin heavy chain isoform 5C and A HIS TAG, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: kinesin, microtubule, motor, transport protein
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm, cytoskeleton : P28738
• Total number of polymer chains: 1
• Total formula weight: 41658.72

Authors

Nitta, R.,Kikkawa, M.,Okada, Y.,Hirokawa, N. (deposition date: 2004-04-19, release date: 2004-08-10, Last modification date: 2023-12-27)

Primary citation

Nitta, R.,Kikkawa, M.,Okada, Y.,Hirokawa, N.
KIF1A Alternately Uses Two Loops to Bind Microtubules
Science, 305:678-683, 2004

PubMed Abstract: The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.

PubMed: 15286375
DOI: 10.1126/science.1096621

Experimental method

X-RAY DIFFRACTION (2.3 Å)