3L1C

Kinesin-14 Protein Ncd, T436S Mutant

Summary for 3L1C

• Entry DOI: 10.2210/pdb3l1c/pdb
• Descriptor: Protein claret segregational, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: kinesin ncd, atp-binding, motor protein
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Cytoplasm, cytoskeleton (Probable): P20480
• Total number of polymer chains: 2
• Total formula weight: 88097.83

Authors

Kull, F.J. (deposition date: 2009-12-11, release date: 2010-08-18, Last modification date: 2023-09-06)

Primary citation

Heuston, E.,Bronner, C.E.,Kull, F.J.,Endow, S.A.
A kinesin motor in a force-producing conformation.
Bmc Struct.Biol., 10:19-19, 2010

PubMed Abstract: Kinesin motors hydrolyze ATP to produce force and move along microtubules, converting chemical energy into work by a mechanism that is only poorly understood. Key transitions and intermediate states in the process are still structurally uncharacterized, and remain outstanding questions in the field. Perturbing the motor by introducing point mutations could stabilize transitional or unstable states, providing critical information about these rarer states.

PubMed: 20602775
DOI: 10.1186/1472-6807-10-19

Experimental method

X-RAY DIFFRACTION (2.75 Å)