Kinesins move along microtubules consuming ATP

Stable Identifier
Reaction [omitted]
Homo sapiens
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Kinesins consume ATP to power the motor which allows them to move along microtubules. The motor region contains highly conserved Switch 1 (SSRSH) and 2 (DLAGSE) motifs which change conformation during ATP hydrolysis (Rice et al. 1999). These form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen by cryo-electron microscopy in human conventional kinesin (Sindelar & Downing 2010) and in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).
Literature References
PubMed ID Title Journal Year
2142332 Evidence that the head of kinesin is sufficient for force generation and motility in vitro

Raff, EC, Goldstein, LS, Yang, JT, Stewart, RJ, Saxton, WM

Science 1990
8602245 Direct observation of single kinesin molecules moving along microtubules

Vale, RD, Romberg, L, Harada, Y, Pierce, DW, Yanagida, T, Funatsu, T

Nature 1996
12368902 Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy

Budny, MJ, Sindelar, CV, Fletterick, R, Cooke, R, Naber, N, Rice, S

Nat Struct Biol 2002
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