PDBsum entry: 1goj

Motor protein

PDB id: 1goj

Contents

Protein chain

354 a.a. *

Ligands

ADP

Metals

_MG

Waters ×114

* Residue conservation analysis

PDB id:

1goj

Name:

Motor protein

Title:

Structure of a fast kinesin: implications for atpase mechanism and interactions with microtubules

Structure:

Kinesin heavy chain. Chain: a. Fragment: motor domain, residues 1-355. Synonym: kinesin. Engineered: yes

Source:

Neurospora crassa. Organism_taxid: 5141. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.3Å R-factor: 0.223 R-free: 0.264

Authors:

Y.-H.Song,A.Marx,J.Muller,G.Woehlke,M.Schliwa,A.Krebs, A.Hoenger,E.Mandelkow

Key ref:

Y.H.Song et al. (2001). Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules. EMBO J, 20, 6213-6225. PubMed id: 11707393 DOI: 10.1093/emboj/20.22.6213

Date:

21-Oct-01 Release date: 30-Nov-01

Protein chain

P48467  (KINH_NEUCR) -  Kinesin heavy chain

Seq: 928 a.a.

Struc: 354 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: microtubule-based movement (1 term)
• Biochemical function: ATP binding (2 terms)

DOI no: 10.1093/emboj/20.22.6213

EMBO J 20:6213-6225 (2001)

PubMed id: 11707393

Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules.

Y.H.Song, A.Marx, J.Müller, G.Woehlke, M.Schliwa, A.Krebs, A.Hoenger, E.Mandelkow.

ABSTRACT

We determined the crystal structure of the motor domain of the fast fungal kinesin from Neurospora crassa (NcKin). The structure has several unique features. (i) Loop 11 in the switch 2 region is ordered and enables one to describe the complete nucleotide-binding pocket, including three inter-switch salt bridges between switch 1 and 2. (ii) Loop 9 in the switch 1 region bends outwards, making the nucleotide-binding pocket very wide. The displacement in switch 1 resembles that of the G-protein ras complexed with its guanosine nucleotide exchange factor. (iii) Loop 5 in the entrance to the nucleotide-binding pocket is remarkably long and interacts with the ribose of ATP. (iv) The linker and neck region is not well defined, indicating that it is mobile. (v) Image reconstructions of ice-embedded microtubules decorated with NcKin show that it interacts with several tubulin subunits, including a central beta-tubulin monomer and the two flanking alpha-tubulin monomers within the microtubule protofilament. Comparison of NcKin with other kinesins, myosin and G-proteins suggests that the rate-limiting step of ADP release is accelerated in the fungal kinesin and accounts for the unusually high velocity and ATPase activity.

Selected figure(s)

Figure 2.
Figure 2 Comparisons between the Sw2 structures of NcKin (black) and Ncd (grey) in ribbon representations. The orientation of the view is the same as in Figure 1. The switch 2 helix 4 and the strand are somewhat extended into the L11 region.

Figure 6.
Figure 6 Comparisons of salt bridges at the -phosphate-sensing region. (A) Stereo view of the superposition of NcKin (dark colour) and RnKin (pale colour). In NcKin, there are three inter-switch salt bridges and in RnKin there is only one. The salt bridge E97 -K188 of RnKin cannot be formed in NcKin because at the corresponding positions there are no charged residues, which are Met99 and Gly191, respectively. (B) Summary of all known salt bridges of known kinesin structures.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2001, 20, 6213-6225) copyright 2001.

Figures were selected by an automated process.