4LNU: Nucleotide-free Kinesin Motor Domain In Complex With Tubulin And A Darpin

Citation:
Abstract
Kinesin-1 is a dimeric ATP-dependent motor protein that moves towards microtubules (+) ends. This movement is driven by two conformations (docked and undocked) of the two motor domains carboxy-terminal peptides (named neck linkers), in correlation with the nucleotide bound to each motor domain. Despite extensive data on kinesin-1, the structural connection between its nucleotide cycle and movement has remained elusive, mostly because the structure of the critical tubulin-bound apo-kinesin state was unknown. Here we report the 2.2 A structure of this complex. From its comparison with detached kinesin-ADP and tubulin-bound kinesin-ATP, we identify three kinesin motor subdomains that move rigidly along the nucleotide cycle. Our data reveal how these subdomains reorient on binding to tubulin and when ATP binds, leading respectively to ADP release and to neck linker docking. These results establish a framework for understanding the transformation of chemical energy into mechanical work by (+) end-directed kinesins.
PDB ID: 4LNUDownload
MMDB ID: 125179
PDB Deposition Date: 2013/7/12
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 2.19  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 4LNU: tetrameric; determined by author and by software (PISA)
Molecular Components in 4LNU
Label Count Molecule
Proteins (4 molecules)
1
Tubulin Alpha Chain
Molecule annotation
1
Tubulin Beta Chain
Molecule annotation
1
Designed Ankyrin Repeat Protein (Darpin) D1
Molecule annotation
1
Kinesin-1 Heavy Chain(Gene symbol: KIF5B)
Molecule annotation
Chemicals (19 molecules)
1
1
2
1
3
11
4
1
5
1
6
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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