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Literature summary for 5.6.1.2 extracted from

  • McNaughton, L.; Tikhonenko, I.; Banavali, N.K.; LeMaster, D.M.; Koonce, M.P.
    A low affinity ground state conformation for the dynein microtubule binding domain (2010), J. Biol. Chem., 285, 15994-16002.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
the active sites for microtubule binding and ATP hydrolysis communicate via conformational changes transduced through a ca. 10 nm length antiparallel coilded-coil stalk, which connects the binding domain to the roughly 300 kDa motor core. A balancing of opposing conformations in the stalk and microtubule binding domain (MTBD) enables modest ling-range interactions arising from ATP-binding in the motor core to induce a relaxation of the MTBD into the stable low affinity state Dictyostelium discoideum

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + a dynein associated with a microtubule at position n = ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end) the active sites for microtubule binding and ATP hydrolysis communicate via conformational changes transduced through a ca. 10 nm length antiparallel coilded-coil stalk, which connects the binding domain to the roughly 300 kDa motor core. A balancing of opposing conformations in the stalk and microtubule binding domain (MTBD) enables modest ling-range interactions arising from ATP-binding in the motor core to induce a reaxation of the MTBD into the stable low affinity state Dictyostelium discoideum

Synonyms

Synonyms Comment Organism
dynein
-
Dictyostelium discoideum