2OWM

Motor domain of Neurospora crassa kinesin-3 (NcKin3)

Summary for 2OWM

• Entry DOI: 10.2210/pdb2owm/pdb
• Descriptor: Related to KINESIN-LIKE PROTEIN KIF1C, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: kinesin; kinesin-3; motor domain; adp; neck linker, motor protein
• Biological source: Neurospora crassa
• Total number of polymer chains: 4
• Total formula weight: 200267.56

Authors

Marx, A.,Muller, J.,Mandelkow, E.-M.,Woehlke, G.,Mandelkow, E. (deposition date: 2007-02-16, release date: 2008-01-29, Last modification date: 2023-08-30)

Primary citation

Marx, A.,Muller, J.,Mandelkow, E.-M.,Woehlke, G.,Bouchet-Marquis, C.,Hoenger, A.,Mandelkow, E.
X-ray Structure and Microtubule Interaction of the Motor Domain of Neurospora crassa NcKin3, a Kinesin with Unusual Processivity
Biochemistry, 47:1848-1861, 2008

PubMed Abstract: Neurospora crassa kinesin NcKin3 belongs to a unique fungal-specific subgroup of small Kinesin-3-related motor proteins. One of its functions appears to be the transport of mitochondria along microtubules. Here, we present the X-ray structure of a C-terminally truncated monomeric construct of NcKin3 comprising the motor domain and the neck linker, and a 3-D image reconstruction of this motor domain bound to microtubules, by cryoelectron microscopy. The protein contains Mg.ADP bound to the active site, yet the structure resembles an ATP-bound state. By comparison with structures of the Kinesin-3 motor Kif1A in different nucleotide states (Kikkawa, M. et al. (2001) Nature (London, U.K.) 411, 439-445), the NcKin3 structure corresponds to the AMPPCP complex of Kif1A rather than the AMPPNP complex. NcKin3-specific differences in the coordination of the nucleotide and asymmetric interactions between adjacent molecules in the crystal are discussed in the context of the unusual kinetics of the dimeric wild-type motor and the monomeric construct used for crystal structure analysis. The NcKin3 motor decorates microtubules at a stoichiometry of one head per alphabeta-tubulin heterodimer, thereby forming an axial periodicity of 8 nm. In spite of unusual extensions at the N-terminus and within flexible loops L2, L8a, and L12 (corresponding to the K-loop of monomeric kinesins), the microtubule binding geometry is similar to that of other members of the kinesin family.

PubMed: 18205396
DOI: 10.1021/bi701483h

Experimental method

X-RAY DIFFRACTION (3.25 Å)