5GSZ

Crystal Structure of the KIF19A Motor Domain Complexed with Mg-ADP

Summary for 5GSZ

• Entry DOI: 10.2210/pdb5gsz/pdb
• Descriptor: Kinesin-like protein KIF19, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: kinesin, motor domain, mg-adp, motor protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 40120.52

Authors

Wang, D.,Nitta, R.,Hirokawa, N. (deposition date: 2016-08-18, release date: 2016-09-28, Last modification date: 2024-10-16)

Primary citation

Wang, D.,Nitta, R.,Morikawa, M.,Yajima, H.,Inoue, S.,Shigematsu, H.,Kikkawa, M.,Hirokawa, N.
Motility and microtubule depolymerization mechanisms of the Kinesin-8 motor, KIF19A
Elife, 5:-, 2016

PubMed Abstract: The kinesin-8 motor, KIF19A, accumulates at cilia tips and controls cilium length. Defective KIF19A leads to hydrocephalus and female infertility because of abnormally elongated cilia. Uniquely among kinesins, KIF19A possesses the dual functions of motility along ciliary microtubules and depolymerization of microtubules. To elucidate the molecular mechanisms of these functions we solved the crystal structure of its motor domain and determined its cryo-electron microscopy structure complexed with a microtubule. The features of KIF19A that enable its dual function are clustered on its microtubule-binding side. Unexpectedly, a destabilized switch II coordinates with a destabilized L8 to enable KIF19A to adjust to both straight and curved microtubule protofilaments. The basic clusters of L2 and L12 tether the microtubule. The long L2 with a characteristic acidic-hydrophobic-basic sequence effectively stabilizes the curved conformation of microtubule ends. Hence, KIF19A utilizes multiple strategies to accomplish the dual functions of motility and microtubule depolymerization by ATP hydrolysis.

PubMed: 27690357
DOI: 10.7554/eLife.18101

Experimental method

X-RAY DIFFRACTION (2.72 Å)