Motor Proteins- Cytoplasmic Dyenin

Descripción

(Molecular Motors) Structural Basis for Biological Function Fichas sobre Motor Proteins- Cytoplasmic Dyenin, creado por gina_evans0312 el 15/12/2013.
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Fichas por gina_evans0312, actualizado hace más de 1 año
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Creado por gina_evans0312 hace alrededor de 11 años
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Resumen del Recurso

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Size of Cytoplasmic Dyenin 350 kDa
Dyenin Superfamily AAA+
Direction of C.Dyenin movement From plus end to minus end
Cargo mRNA, proteins, viruses- it varies
Role of Multiple Light Chain Where cargo binds
No of heavy chains 2
AAA+ domains Form a hexameric motor domain
Role of Linker domain Dimerises protein
Coiled coil Links AAA+ motor heads to microtubule binding site
N-terminus Light chains, dimerisation and cargo binding
C terminus AAA+ motors, tubulin binding and linking coiled coil stalk
Location of ATP binding AAA+ domains
Binding of ATP changes Relative positions of linker domains and coiled coil
ATP binding causes _ of MTBD Weakening of MTBD to tubulin
No of ATP req'd Unclear
Distance moved by Dyenin heads 16nm- but it varies a lot
Largest known 'step' of head 30 nm
Backwards movement Possible
Movement onto other microtubules Allows it to pass kinesin (kinesin can't change M.T's)
Mutant with non-functioning ATP head Still moved, but slowly and with no powerstroke
Co-ordination of Dyenin movement Much less co-ordinated than kinesin
Mechanism of movement Hand over Hand model
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