5DJN

Crystal structure of the Kinesin-3 KIF13A NC-CC1 mutant - Deletion of P390

Summary for 5DJN

• Entry DOI: 10.2210/pdb5djn/pdb
• Related: 5DJN
• Descriptor: Kinesin-like protein (2 entities in total)
• Functional Keywords: coil-coil, transport protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 21406.12

Authors

Ren, J.Q.,Feng, W. (deposition date: 2015-09-02, release date: 2015-12-30, Last modification date: 2024-03-20)

Primary citation

Ren, J.,Huo, L.,Wang, W.,Zhang, Y.,Li, W.,Lou, J.,Xu, T.,Feng, W.
Structural Correlation of the Neck Coil with the Coiled-coil (CC1)-Forkhead-associated (FHA) Tandem for Active Kinesin-3 KIF13A
J.Biol.Chem., 291:3581-3594, 2016

PubMed Abstract: Processive kinesin motors often contain a coiled-coil neck that controls the directionality and processivity. However, the neck coil (NC) of kinesin-3 is too short to form a stable coiled-coil dimer. Here, we found that the coiled-coil (CC1)-forkhead-associated (FHA) tandem (that is connected to NC by Pro-390) of kinesin-3 KIF13A assembles as an extended dimer. With the removal of Pro-390, the NC-CC1 tandem of KIF13A unexpectedly forms a continuous coiled-coil dimer that can be well aligned into the CC1-FHA dimer. The reverse introduction of Pro-390 breaks the NC-CC1 coiled-coil dimer but provides the intrinsic flexibility to couple NC with the CC1-FHA tandem. Mutations of either NC, CC1, or the FHA domain all significantly impaired the motor activity. Thus, the three elements within the NC-CC1-FHA tandem of KIF13A are structurally interrelated to form a stable dimer for activating the motor. This work also provides the first direct structural evidence to support the formation of a coiled-coil neck by the short characteristic neck domain of kinesin-3.

PubMed: 26680000
DOI: 10.1074/jbc.M115.689091

Experimental method

X-RAY DIFFRACTION (2.82 Å)