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Literature summary 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)

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.6.1.2 380000
-
 cytoplasmic dynein motor domain Dictyostelium discoideum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.1.2 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)
-
 ?
5.6.1.2 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

EC Number Organism UniProt Comment Textmining
5.6.1.2 Chlamydomonas reinhardtii
-
-
-
5.6.1.2 Dictyostelium discoideum
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.2 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)
-
 ?
5.6.1.2 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

EC Number Synonyms Comment Organism
5.6.1.2 flagellar dynein-c
-
 Chlamydomonas reinhardtii

General Information

EC Number General Information Comment Organism
5.6.1.2 evolution dyneins are members of the AAA+ superfamily of ring-shaped enzymes Chlamydomonas reinhardtii
5.6.1.2 evolution dyneins are members of the AAA+ superfamily of ring-shaped enzymes Dictyostelium discoideum
5.6.1.2 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
5.6.1.2 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