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5ZBR

Crystal Structure of Kinesin-3 KIF13B motor domain in AMPPNP form

Summary for 5ZBR
Entry DOI10.2210/pdb5zbr/pdb
DescriptorKinesin family member 13B, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordskinesin, atpase, transport protein
Biological sourceRattus norvegicus (Rat)
Total number of polymer chains3
Total formula weight126652.82
Authors
Ren, J.Q.,Wang, S.,Feng, W. (deposition date: 2018-02-12, release date: 2018-05-30, Last modification date: 2023-11-22)
Primary citationRen, J.,Zhang, Y.,Wang, S.,Huo, L.,Lou, J.,Feng, W.
Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement.
J. Mol. Biol., 430:2030-2041, 2018
Cited by
PubMed Abstract: Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)-NL-NC tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD-NL-NC structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3.
PubMed: 29752968
DOI: 10.1016/j.jmb.2018.05.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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