4HNA

Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN

Summary for 4HNA

• Entry DOI: 10.2210/pdb4hna/pdb
• Descriptor: Tubulin alpha chain, Tubulin beta chain, DESIGNED ANKYRIN REPEAT PROTEIN (DARPIN) D2, ... (10 entities in total)
• Functional Keywords: alpha-tubulin, beta-tubulin, darpin, gtpase, kinesin, microtubule, tubulin, motor protein
• Biological source: ARTIFICIAL GENE; More
• Cellular location: Cytoplasm, cytoskeleton : D0VWZ0 D0VWY9 P33176
• Total number of polymer chains: 4
• Total formula weight: 159175.07

Authors

Gigant, B.,Knossow, M. (deposition date: 2012-10-19, release date: 2013-06-12, Last modification date: 2023-09-20)

Primary citation

Gigant, B.,Wang, W.,Dreier, B.,Jiang, Q.,Pecqueur, L.,Pluckthun, A.,Wang, C.,Knossow, M.
Structure of a kinesin-tubulin complex and implications for kinesin motility.
Nat.Struct.Mol.Biol., 20:1001-1007, 2013

PubMed Abstract: The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to αβ-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken.

PubMed: 23872990
DOI: 10.1038/nsmb.2624

Experimental method

X-RAY DIFFRACTION (3.19 Å)