PDBsum entry 4lnu

Cell cycle/motor protein

PDB id: 4lnu

Contents

Protein chains

434 a.a.

431 a.a.

157 a.a.

309 a.a.

Ligands

GTP

SO4 ×11

GDP

MES

GOL ×4

Metals

_MG

Waters ×633

References listed in PDB file

Key reference

• Title: The structure of apo-Kinesin bound to tubulin links the nucleotide cycle to movement.
• Authors: L.Cao, W.Wang, Q.Jiang, C.Wang, M.Knossow, B.Gigant.
• Ref.: Nat Commun, 2014, 5, 5364. [DOI no: 10.1038/ncomms6364]
• PubMed id: 25395082

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 Å 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.