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Literature summary for 5.6.1.3 extracted from

  • Alonso, M.C.; Drummond, D.R.; Kain, S.; Hoeng, J.; Amos, L.; Cross, R.A.
    An ATP gate controls tubulin binding by the tethered head of kinesin-1 (2007), Science, 316, 120-123.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.3

Activating Compound

Activating Compound Comment Organism Structure
microtubule half-maximal activation at 0.00039 mM Neurospora crassa
microtubule half-maximal activation at 2.03 mM Rattus norvegicus
tubulin heterodimer half-maximal activation at 0.00129 mM for Schizosaccharamyces pombe tubulin, at 0.00062 mM for rat brain tubulin Neurospora crassa
tubulin heterodimer half-maximal activation at 0.00203 mM for Schizosaccharamyces pombe tubulin, at 0.00086 mM for brain tubulin Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
 Rattus norvegicus ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head ?
ATP + H2O + a kinesin associated with a microtubule at position n
-
 Neurospora crassa ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head ?

Subunits

Subunits Comment Organism
More unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate. With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In presence of adenylyl-imidodiphosphate, each kinesin-1 dimer binds two tubulin heterodimers. Existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head Rattus norvegicus
More unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate. With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In presence of adenylyl-imidodiphosphate, each kinesin-1 dimer binds two tubulin heterodimers. Existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head Neurospora crassa