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Literature summary for 5.6.1.2 extracted from

  • Roberts, A.J.; Malkova, B.; Walker, M.L.; Sakakibara, H.; Numata, N.; Kon, T.; Ohkura, R.; Edwards, T.A.; Knight, P.J.; Sutoh, K.; Oiwa, K.; Burgess, S.A.
    ATP-driven remodeling of the linker domain in the dynein motor (2012), Structure, 20, 1670-1680.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Chlamydomonas reinhardtii
crystal structure analysis Dictyostelium discoideum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Dictyostelium discoideum 5737
-
flagellum
-
Chlamydomonas reinhardtii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Chlamydomonas reinhardtii
Mg2+ required Dictyostelium discoideum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
380000
-
cytoplasmic dynein motor domain Dictyostelium discoideum

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 Chlamydomonas reinhardtii
-
ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
?
ATP + H2O + a dynein associated with a microtubule at position n Dictyostelium discoideum
-
ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii
-
-
-
Dictyostelium discoideum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native native dynein-c from flagella Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a dynein associated with a microtubule at position n
-
Chlamydomonas reinhardtii ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
?
ATP + H2O + a dynein associated with a microtubule at position n
-
Dictyostelium discoideum ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
?

Synonyms

Synonyms Comment Organism
flagellar dynein-c
-
Chlamydomonas reinhardtii

General Information

General Information Comment Organism
evolution dyneins are members of the AAA+ superfamily of ring-shaped enzymes Chlamydomonas reinhardtii
evolution dyneins are members of the AAA+ superfamily of ring-shaped enzymes Dictyostelium discoideum
additional information dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. ATP-driven remodeling of the linker domain in the dynein motor, structure-function analysis of the cytoplasmic dynein motor domain, motor mechanism, overview. Driving sliding between microtubules with energy that is supplied by interactions with the AAA+ modules. Conserved architecture of the head domains of cytoplasmic dynein, an open nucleotide-binding pocket at AAA1 is an intrinsic feature of dynein structure in the absence of nucleotide. Modeling Dictyostelium discoideum
additional information dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. ATP-driven remodeling of the linker domain in the dynein motor, structure-function analysis of the flagellar dynein-c, motor mechanism, overview. Driving sliding between microtubules with energy that is supplied by interactions with the AAA+ modules. Architecture of the head domains of axonemal dynein-c comprising an asymmetric ring-like structure with the linker domain arching over one face. Modeling Chlamydomonas reinhardtii