5MIO

KIF2C-DARPIN FUSION PROTEIN BOUND TO TUBULIN

Summary for 5MIO

• Entry DOI: 10.2210/pdb5mio/pdb
• Descriptor: Tubulin alpha-1B chain, Tubulin beta chain, Kinesin-like protein KIF2C,KIF2C FUSED TO A DARPIN,KIF2C FUSED TO A DARPIN, ... (8 entities in total)
• Functional Keywords: kinesin-13 microtubule atpase motor protein, motor protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 164235.39

Authors

Wang, W.,Gigant, B. (deposition date: 2016-11-28, release date: 2017-07-19, Last modification date: 2024-10-23)

Primary citation

Wang, W.,Cantos-Fernandes, S.,Lv, Y.,Kuerban, H.,Ahmad, S.,Wang, C.,Gigant, B.
Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.
Nat Commun, 8:70-70, 2017

PubMed Abstract: Kinesin-13s are critical microtubule regulators which induce microtubule disassembly in an ATP dependent manner. To clarify their mechanism, we report here the crystal structure of a functional construct of the kinesin-13 Kif2C/MCAK in an ATP-like state and bound to the αβ-tubulin heterodimer, a complex mimicking the species that dissociates from microtubule ends during catalytic disassembly. Our results picture how Kif2C stabilizes a curved tubulin conformation. The Kif2C α4-L12-α5 region undergoes a remarkable 25° rotation upon tubulin binding to target the αβ-tubulin hinge. This movement leads the β5a-β5b motif to interact with the distal end of β-tubulin, whereas the neck and the KVD motif, two specific elements of kinesin-13s, target the α-tubulin distal end. Taken together with the study of Kif2C mutants, our data suggest that stabilization of a curved tubulin is an important contribution to the Kif2C mechanism.Kinesin-13s are microtubule depolymerizing enzymes. Here the authors present the crystal structure of a DARPin fused construct comprising the short neck region and motor domain of kinesin-13 in complex with an αβ-tubulin heterodimer, which shows that kinesin-13 functions by stabilizing a curved tubulin conformation.

PubMed: 28694425
DOI: 10.1038/s41467-017-00091-9

Experimental method

X-RAY DIFFRACTION (3.19 Å)