1CZ7

THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS

Summary for 1CZ7

• Entry DOI: 10.2210/pdb1cz7/pdb
• Related: 2NCD
• Descriptor: MICROTUBULE MOTOR PROTEIN NCD, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: ncd crystal structure, microtubule motors, kinesin superfamily, contractile protein
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Cytoplasm, cytoskeleton (Probable): P20480
• Total number of polymer chains: 4
• Total formula weight: 186274.04

Authors

Kozielski, F.K.,De Bonis, S.,Burmeister, W.,Cohen-Addad, C.,Wade, R. (deposition date: 1999-09-01, release date: 1999-11-05, Last modification date: 2024-02-07)

Primary citation

Kozielski, F.,De Bonis, S.,Burmeister, W.P.,Cohen-Addad, C.,Wade, R.H.
The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations.
Structure Fold.Des., 7:1407-1416, 1999

PubMed Abstract: The kinesin superfamily of microtubule-associated motor proteins are important for intracellular transport and for cell division in eukaryotes. Conventional kinesins have the motor domain at the N terminus of the heavy chain and move towards the plus end of microtubules. The ncd protein is necessary for chromosome segregation in meiosis. It belongs to a subfamily of kinesins that have the motor domain at the C terminus and move towards the minus end of microtubules.

PubMed: 10574799
DOI: 10.1016/S0969-2126(00)80030-1

Experimental method

X-RAY DIFFRACTION (2.9 Å)