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Literature summary for 5.6.1.2 extracted from

  • Uchimura, S.; Fujii, T.; Takazaki, H.; Ayukawa, R.; Nishikawa, Y.; Minoura, I.; Hachikubo, Y.; Kurisu, G.; Sutoh, K.; Kon, T.; Namba, K.; Muto, E.
    A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation (2015), J. Cell Biol., 208, 211-222 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.2

Cloned(Commentary)

Cloned (Comment) Organism
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 Dictyostelium discoideum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Dictyostelium discoideum 5737
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a dynein associated with a microtubule at position n Dictyostelium discoideum dynein is a motor protein that moves on microtubules using the energy of adenosine triphosphate hydrolysis ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
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 ?

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum P34036 dynein heavy chain
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Purification (Commentary)

Purification (Comment) Organism
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 Dictyostelium discoideum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a dynein associated with a microtubule at position n dynein is a motor protein that moves on microtubules using the energy of adenosine triphosphate hydrolysis Dictyostelium discoideum ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
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 ?
ATP + H2O + a dynein associated with a microtubule at position n dynein is a motor protein that moves on microtubules using the energy of adenosine triphosphate hydrolysis. The alpha-tubulin residues R403 and E416 are critical for ATPase activation and directional movement of dynein. These residues form salt bridges with the residues in the dynein microtubule-binding domain that work in concert to induce registry change in the stalk coiled coil and activate the ATPase. The R403-E3390 salt bridge functions as a switch for this mechanism because of its reversed charge relative to other residues at the interface Dictyostelium discoideum ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
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 ?

General Information

General Information Comment Organism
physiological function dynein is a motor protein that moves on microtubules using the energy of adenosine triphosphate hydrolysis Dictyostelium discoideum