7A3Z

OSM-3 kinesin motor domain complexed with Mg.ADP

Summary for 7A3Z

• Entry DOI: 10.2210/pdb7a3z/pdb
• Descriptor: Osmotic avoidance abnormal protein 3, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: kinesin-2, kif17, motor domain, atpase, motor protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 41559.93

Authors

Varela, F.P.,Menetrey, J.,Gigant, B. (deposition date: 2020-08-19, release date: 2021-02-03, Last modification date: 2024-01-31)

Primary citation

Varela, P.F.,Chenon, M.,Velours, C.,Verhey, K.J.,Menetrey, J.,Gigant, B.
Structural snapshots of the kinesin-2 OSM-3 along its nucleotide cycle: implications for the ATP hydrolysis mechanism.
Febs Open Bio, 11:564-577, 2021

PubMed Abstract: Motile kinesins are motor proteins that translocate along microtubules as they hydrolyze ATP. They share a conserved motor domain which harbors both ATPase and microtubule-binding activities. An ATP hydrolysis mechanism involving two water molecules has been proposed based on the structure of the kinesin-5 Eg5 bound to an ATP analog. Whether this mechanism is general in the kinesin superfamily remains uncertain. Here, we present structural snapshots of the motor domain of OSM-3 along its nucleotide cycle. OSM-3 belongs to the homodimeric kinesin-2 subfamily and is the Caenorhabditis elegans homologue of human KIF17. OSM-3 bound to ADP or devoid of a nucleotide shows features of ADP-kinesins with a docked neck linker. When bound to an ATP analog, OSM-3 adopts a conformation similar to those of several ATP-like kinesins, either isolated or bound to tubulin. Moreover, the OSM-3 nucleotide-binding site is virtually identical to that of ATP-like Eg5, demonstrating a shared ATPase mechanism. Therefore, our data extend to kinesin-2 the two-water ATP hydrolysis mechanism and further suggest that it is universal within the kinesin superfamily. PROTEIN DATABASE ENTRIES: 7A3Z, 7A40, 7A5E.

PubMed: 33513284
DOI: 10.1002/2211-5463.13101

Experimental method

X-RAY DIFFRACTION (2.095 Å)