Literature summary for 5.6.1.3 extracted from

Shang, Z.; Zhou, K.; Xu, C.; Csencsits, R.; Cochran, J.C.; Sindelar, C.V.
High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation (2014), eLife, 3, e04686.

Search for more literature for 5.6.1.3

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis of ubiquitous kinesin motor domain and kinesin motor domain with docked neck linker, PDB IDs 1BG2 and 1MKJ, respectively	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
microtubule	structure of the kinesin-microtubule complex, overview	Homo sapiens	5874	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + a kinesin associated with a microtubule at position n	Homo sapiens	-	ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P33176	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + a kinesin associated with a microtubule at position n	-	Homo sapiens	ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)	-	?
ATP + H2O + a kinesin associated with a microtubule at position n	-	Homo sapiens	ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)	analysis of structures of ADP-bound kinesin	?

Subunits

Subunits	Comment	Organism
dimer	Kinesin-1 dimerizes via an extended stalk domain that forms a coiled coil, so that the two catalytic motor domains are situated at one end of the coiled-coil, while cargo-binding domains are found at the opposite end. During active motility, the dimerized motor domains take alternating, eight nanometer steps toward the microtubule plus end, tracking along single protofilaments, structure overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
conventional kinesin	-	Homo sapiens
kinesin-1	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	conventional kinesin is the founding member of a superfamily of molecular motors that use the energy of ATP hydrolysis to transport cargo along microtubules, serving essential roles in a wide variety of cellular processes, most notably mitosis and neuronal transport	Homo sapiens
additional information	atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-electronmicrosopy reconstructions at 5-6 A resolution, overview. Microtubule attachment, mediated by a universally conserved linchpin residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP, modeling of crystal structures of ADP-bound enzyme and mechanism. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's neck linker element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kinesin dimer gate each other to promote coordinated stepping along microtubules. Kinesin-1 dimerizes via an extended stalk domain that forms a coiled coil, so that the two catalytic motor domains are situated at one end of the coiled-coil, while cargo-binding domains are found at the opposite end. During active motility, the dimerized motor domains take alternating, eight nanometer steps toward the microtubule plus end, tracking along single protofilaments	Homo sapiens
physiological function	microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)