Reactome | All kinesins contain a motor domain or head, the position va...

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created	[InstanceEdit:990475] Jupe, S, 2010-11-03
dbId	990477
displayName	All kinesins contain a motor domain or head, the position va...
literatureReference	[LiteratureReference:990486] Crystal structure of the kinesin motor domain reveals a structural similarity to myosin [LiteratureReference:990501] Crystal structure of the motor domain of the kinesin-related motor ncd [LiteratureReference:990508] Structural mechanism of muscle contraction [LiteratureReference:990512] ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
schemaClass	Summation
text	All kinesins contain a motor domain or head, the position varies but it is structurally highly conserved (Kull et al. 1996, Sablin et al. 1996). The microtubule-binding site includes structural elements which interact with tubulin and undergo movement between the ADP and ATP bound states. The highly conserved switch I (SSRSH) and II (DLAGSE) motifs, which change in conformation during the ATP hydrolysis cycle, 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 in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).

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