4EGX

Crystal structure of KIF1A CC1-FHA tandem

Summary for 4EGX

• Entry DOI: 10.2210/pdb4egx/pdb
• Related: 4EJQ
• Descriptor: Kinesin-like protein KIF1A, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (4 entities in total)
• Functional Keywords: fha domain, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: Q12756
• Total number of polymer chains: 4
• Total formula weight: 84255.00

Authors

Yu, J.,Huo, L.,Yue, Y.,Xu, T.,Zhang, M.,Feng, W. (deposition date: 2012-04-02, release date: 2012-10-03, Last modification date: 2023-11-08)

Primary citation

Huo, L.,Yue, Y.,Ren, J.,Yu, J.,Liu, J.,Yu, Y.,Ye, F.,Xu, T.,Zhang, M.,Feng, W.
The CC1-FHA Tandem as a Central Hub for Controlling the Dimerization and Activation of Kinesin-3 KIF1A
Structure, 20:1550-1561, 2012

PubMed Abstract: Kinesin-3 KIF1A plays prominent roles in axonal transport and synaptogenesis. KIF1A adopts a monomeric form in vitro but acts as a processive dimer in vivo. The mechanism underlying the motor dimerization is poorly understood. Here, we find that the CC1-FHA tandem of KIF1A exists as a stable dimer. The structure of CC1-FHA reveals that the linker between CC1 and FHA unexpectedly forms a β-finger hairpin, which integrates CC1 with FHA assembling a CC1-FHA homodimer. More importantly, dissociation of the CC1-FHA dimer unleashes CC1 and the β-finger, which are both essential for the motor inhibition. Thus, dimerization of the CC1-FHA tandem not only promotes the KIF1A dimer formation but also may trigger the motor activity via sequestering the CC1/β-finger region. The CC1-FHA tandem likely functions as a hub for controlling the dimerization and activation of KIF1A, which may represent a new paradigm for the kinesin regulation shared by other kinesin-3 motors.

PubMed: 22863567
DOI: 10.1016/j.str.2012.07.002

Experimental method

X-RAY DIFFRACTION (2.51 Å)