Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain.

@article{Shiozawa2004StructureOT,
  title={Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain.},
  author={Kumiko Shiozawa and Nobuo Maita and Kentaro Tomii and Azusa Seto and Natsuko Goda and Y. Akiyama and Toshiyuki Shimizu and Masahiro Shirakawa and Hidekazu Hiroaki},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 48},
  pages={50060-8}
}
Peroxisomes are responsible for several pathways in primary metabolism, including beta-oxidation and lipid biosynthesis. PEX1 and PEX6 are hexameric AAA-type ATPases, both of which are indispensable in targeting over 50 peroxisomal resident proteins from the cytosol to the peroxisomes. Although the tandem AAA-ATPase domains in the central region of PEX1 and PEX6 are highly similar, the N-terminal sequences are unique. To better understand the distinct molecular function of these two proteins… CONTINUE READING