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Literature summary for 3.6.4.B1 extracted from

  • Vinogradova, M.V.; Malanina, G.G.; Reddy, V.S.; Reddy, A.S.; Fletterick, R.J.
    Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein (2008), J. Struct. Biol., 163, 76-83.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli of fragment encoding the potato KCBP from amino acids 884-1252, which include the motor core and the C-terminal extension containing the calmodulin-binding motif Solanum tuberosum

Crystallization (Commentary)

Crystallization (Comment) Organism
four structures of the fragment encoding the potato KCBP from amino acids 884-1252, which include the motor core and the C-terminal extension containing the calmodulin-binding motif. The kinesin motor is in the ATP-like conformation, but loop 11 exhibits different conformational states, both ordered and disordered. When structured, loop 11 adds three additional helical turns to the N-terminal part of the following helix alpha4. Positioning of the calmodulin binding helix is not decided by crystal packing forces but is determined by the conformational state of the motor Solanum tuberosum

Organism

Organism UniProt Comment Textmining
Solanum tuberosum
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isoform KCBP
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Subunits

Subunits Comment Organism
More in kinesin-like calmodulin binding protein, calmodulin binds to helix alpha4 and inserts itself between the motor and the microtubule. Positioning of the calmodulin binding helix is not decided by crystal packing forces but is determined by the conformational state of the motor Solanum tuberosum