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

PDB id:

4lnu

Name:

Cell cycle/motor protein

Title:

Nucleotide-free kinesin motor domain in complex with tubulin and a darpin

Structure:

Tubulin alpha chain. Chain: a. Tubulin beta chain. Chain: b. Designed ankyrin repeat protein (darpin) d1. Chain: d. Engineered: yes. Kinesin-1 heavy chain. Chain: k.

Source:

Ovis aries. Sheep. Organism_taxid: 9940. Organ: brain. Artificial gene. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens.

Resolution:

2.19Å R-factor: 0.157 R-free: 0.195

Authors:

L.Cao,B.Gigant,M.Knossow

Key ref:

L.Cao et al. (2014). The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement. Nat Commun, 5, 5364. PubMed id: 25395082 DOI: 10.1038/ncomms6364

Date:

12-Jul-13 Release date: 03-Dec-14

Protein chain

W5QC38  (W5QC38_SHEEP) -  Tubulin alpha chain from Ovis aries

Seq: 454 a.a.

Struc: 434 a.a.*

Protein chain

D0VWY9  (D0VWY9_SHEEP) -  Tubulin beta chain from Ovis aries

Seq: 445 a.a.

Struc: 431 a.a.*

Protein chain

No UniProt id for this chain

Struc: 157 a.a.

Protein chain

P33176  (KINH_HUMAN) -  Kinesin-1 heavy chain from Homo sapiens

Seq: 963 a.a.

Struc: 309 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

DOI no: 10.1038/ncomms6364

Nat Commun 5:5364 (2014)

PubMed id: 25395082

The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement.

L.Cao, W.Wang, Q.Jiang, C.Wang, M.Knossow, B.Gigant.

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.