期刊
EMBO JOURNAL
卷 23, 期 7, 页码 1422-1432出版社
WILEY
DOI: 10.1038/sj.emboj.7600165
关键词
crystal; depolymerization; kinesin; microtubule; structure
资金
- NIAMS NIH HHS [P01-AR42895, P01 AR042895] Funding Source: Medline
- NIGMS NIH HHS [R01 GM052468, R37 GM052468, GM52468] Funding Source: Medline
With their ability to depolymerize microtubules (MTs), KinI kinesins are the rogue members of the kinesin family. Here we present the 1.6 Angstrom 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 NIT 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.
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