Article
- The EMBO Journal (2004) 23, 1422 - 1432
- doi:10.1038/sj.emboj.7600165
Published online: 18 March 2004
Subject Categories:
Structure of a kinesin microtubule depolymerization machine
Krista Shipley1, Mohammad Hekmat-Nejad2, Jennifer Turner3,a, Carolyn Moores4,b, Robert Anderson2, Ronald Milligan4, Roman Sakowicz2 and Robert Fletterick3
- Graduate Group in Biophysics, University of California, San Francisco, CA, USA
- Cytokinetics Inc., South San Francisco, CA, USA
- Department of Biochemistry/Biophysics, University of California, San Francisco, CA, USA
- Department of Cell Biology, The Scripps Research Institute, La Jolla, CA, USA
Correspondence to:
Robert Fletterick, Department of Biochemistry & Biophysics, University of California, GH Rm. S412E, 600 16th Street, Suite #2240, San Francisco, CA, 94143-2240, USA. Tel.: +1 415 476 5080; Fax: +1 415 476 1902; E-mail: flett@msg.ucsf.edu
aPresent address: Department of Biology, Box 731 Vassar College, 124 Raymond Avenue, Poughkeepsie, NY 12604-0731, USA
bPresent address: School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK
Received 12 December 2003; Accepted 18 February 2004
Abstract
With their ability to depolymerize microtubules (MTs), KinI kinesins are the rogue members of the kinesin family. Here we present the 1.6 Å 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.
Keywords:
- crystal,
- depolymerization,
- kinesin,
- microtubule,
- structure
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