PDBsum entry 3j8x

Motor protein/structural protein

PDB id: 3j8x

Contents

Protein chains

316 a.a.

430 a.a.

431 a.a.

Ligands

GTP

GDP

PDB id:

3j8x

Name:

Motor protein/structural protein

Title:

High-resolution structure of no-nucleotide kinesin on microtubules

Structure:

Kinesin-1 heavy chain. Chain: k. Fragment: truncated catalytic head domain (monomeric, unp residues 1- 349). Synonym: conventional kinesin heavy chain, ubiquitous kinesin heavy chain, ukhc. Engineered: yes. Tubulin alpha-1b chain. Chain: a.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kif5b, kns, kns1. Expressed in: escherichia coli. Expression_system_taxid: 562. Sus scrofa. Pig. Organism_taxid: 9823.

Authors:

Z.Shang,K.Zhou,C.Xu,R.Csencsits,J.C.Cochran,C.V.Sindelar

Key ref:

Z.Shang et al. (2014). High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation. Elife, 3, e04686. PubMed id: 25415053 DOI: 10.7554/eLife.04686

Date:

20-Nov-14 Release date: 10-Dec-14

Protein chain

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

Seq: 963 a.a.

Struc: 316 a.a.*

Protein chain

Q2XVP4  (TBA1B_PIG) -  Tubulin alpha-1B chain from Sus scrofa

Seq: 451 a.a.

Struc: 430 a.a.

Protein chain

F2Z5B2  (F2Z5B2_PIG) -  Tubulin beta chain from Sus scrofa

Seq: 425 a.a.

Struc: 431 a.a.*

* PDB and UniProt seqs differ at 16 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.6.5.- - ?????
• Enzyme class 2: Chains K, B: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.7554/eLife.04686

Elife 3:e04686 (2014)

PubMed id: 25415053

High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation.

Z.Shang, K.Zhou, C.Xu, R.Csencsits, J.C.Cochran, C.V.Sindelar.

ABSTRACT

Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes. We obtained insight into this process by developing atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-EM reconstructions at 5-6 Å resolution. By comparing these models with existing X-ray structures of ADP-bound kinesin, we infer a mechanistic scheme in which microtubule attachment, mediated by a universally conserved 'linchpin' residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's 'neck linker' element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kinesin dimer 'gate' each other to promote coordinated stepping along microtubules.