PDBsum entry 1ry6

Transport protein

PDB id: 1ry6

Contents

Protein chain

319 a.a. *

Ligands

SO4

Waters ×306

* Residue conservation analysis

PDB id:

1ry6

Name:

Transport protein

Title:

Crystal structure of internal kinesin motor domain

Structure:

Internal kinesin. Chain: a. Fragment: atpase 'motor' domain (residues 68-396). Engineered: yes

Source:

Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Gene: pfl2165w. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.207 R-free: 0.231

Authors:

K.Shipley,M.Hekmat-Nejad,J.Turner,C.Moores,R.Anderson,R.Milligan, R.Sakowicz,R.Fletterick

Key ref:

K.Shipley et al. (2004). Structure of a kinesin microtubule depolymerization machine. EMBO J, 23, 1422-1432. PubMed id: 15029249 DOI: 10.1038/sj.emboj.7600165

Date:

19-Dec-03 Release date: 13-Apr-04

Protein chain

Q8I4Y0  (Q8I4Y0_PLAF7) -  Kinesin-13, putative from Plasmodium falciparum (isolate 3D7)

Seq: 1326 a.a.

Struc: 319 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/sj.emboj.7600165

EMBO J 23:1422-1432 (2004)

PubMed id: 15029249

Structure of a kinesin microtubule depolymerization machine.

K.Shipley, M.Hekmat-Nejad, J.Turner, C.Moores, R.Anderson, R.Milligan, R.Sakowicz, R.Fletterick.

ABSTRACT

With their ability to depolymerize microtubules (MTs), KinI kinesins are the rogue members of the kinesin family. Here we present the 1.6 A crystal structure of a KinI motor core from Plasmodium falciparum, which is sufficient for depolymerization in vitro. Unlike all published kinesin structures to date, nucleotide is not present, and there are noticeable differences in loop regions L6 and L10 (the plus-end tip), L2 and L8 and in switch II (L11 and helix4); otherwise, the pKinI structure is very similar to previous kinesin structures. KinI-conserved amino acids were mutated to alanine, and studied for their effects on depolymerization and ATP hydrolysis. Notably, mutation of three residues in L2 appears to primarily affect depolymerization, rather than general MT binding or ATP hydrolysis. The results of this study confirm the suspected importance of loop 2 for KinI function, and provide evidence that KinI is specialized to hydrolyze ATP after initiating depolymerization.

Selected figure(s)

Figure 2.
Figure 2 Comparison of pKinI with the most structurally similar gliding motor NCD. Common elements are shown in gray, differing pKinI parts in red and differing NCD parts in blue. The sulfate ion that marks the -phosphate of ADP is shown in yellow. The largest differences are the length of L2, the positioning of the 'tip' (L6 and L10), the direction of L8 and the unusual stability of the switch II region (L11- 4).

Figure 5.
Figure 5 Location of pKinI amino-acid substitutions. Red spheres mark the three residues and two-residue triplets (K40/V41/D42 and K268/E269/C270) that were mutated to alanine and assayed for their effects on ATP hydrolysis and MT depolymerization.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2004, 23, 1422-1432) copyright 2004.

Figures were selected by an automated process.