1GOJ

Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules

Summary for 1GOJ

• Entry DOI: 10.2210/pdb1goj/pdb
• Descriptor: KINESIN HEAVY CHAIN, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: kinesin, motor protein, atpase, neurospora crassa
• Biological source: NEUROSPORA CRASSA
• Cellular location: Cytoplasm, cytoskeleton (Probable): P48467
• Total number of polymer chains: 1
• Total formula weight: 39244.34

Authors

Song, Y.-H.,Marx, A.,Muller, J.,Woehlke, G.,Schliwa, M.,Krebs, A.,Hoenger, A.,Mandelkow, E. (deposition date: 2001-10-21, release date: 2001-11-30, Last modification date: 2023-12-13)

Primary citation

Song, Y.-H.,Marx, A.,Muller, J.,Woehlke, G.,Schliwa, M.,Krebs, A.,Hoenger, A.,Mandelkow, E.
Structure of a Fast Kinesin: Implications for ATPase Mechanism and Interactions with Microtubules
Embo J., 20:6213-, 2001

PubMed Abstract: We determined the crystal structure of the motor domain of the fast fungal kinesin from Neurospora crassa (NcKin). The structure has several unique features. (i) Loop 11 in the switch 2 region is ordered and enables one to describe the complete nucleotide-binding pocket, including three inter-switch salt bridges between switch 1 and 2. (ii) Loop 9 in the switch 1 region bends outwards, making the nucleotide-binding pocket very wide. The displacement in switch 1 resembles that of the G-protein ras complexed with its guanosine nucleotide exchange factor. (iii) Loop 5 in the entrance to the nucleotide-binding pocket is remarkably long and interacts with the ribose of ATP. (iv) The linker and neck region is not well defined, indicating that it is mobile. (v) Image reconstructions of ice-embedded microtubules decorated with NcKin show that it interacts with several tubulin subunits, including a central beta-tubulin monomer and the two flanking alpha-tubulin monomers within the microtubule protofilament. Comparison of NcKin with other kinesins, myosin and G-proteins suggests that the rate-limiting step of ADP release is accelerated in the fungal kinesin and accounts for the unusually high velocity and ATPase activity.

PubMed: 11707393
DOI: 10.1093/EMBOJ/20.22.6213

Experimental method

X-RAY DIFFRACTION (2.3 Å)