1RY6

Crystal Structure of Internal Kinesin Motor Domain

1RY6 の概要

• エントリーDOI: 10.2210/pdb1ry6/pdb
• 分子名称: INTERNAL KINESIN, SULFATE ION (3 entities in total)
• 機能のキーワード: kinesin motor domain, nucleotide-free, transport protein
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40857.91

構造登録者

Shipley, K.,Hekmat-Nejad, M.,Turner, J.,Moores, C.,Anderson, R.,Milligan, R.,Sakowicz, R.,Fletterick, R. (登録日: 2003-12-19, 公開日: 2004-04-13, 最終更新日: 2023-09-20)

主引用文献

Shipley, K.,Hekmat-Nejad, M.,Turner, J.,Moores, C.,Anderson, R.,Milligan, R.,Sakowicz, R.,Fletterick, R.
Structure of a kinesin microtubule depolymerization machine.
Embo J., 23:1422-1432, 2004

PubMed 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.

PubMed: 15029249
DOI: 10.1038/sj.emboj.7600165

実験手法

X-RAY DIFFRACTION (1.6 Å)