title: Crystallographic characterization of the N-terminal domain of PEX1.
abstract: Peroxisomal enzymes are responsible for several primary metabolism pathways, including beta-oxidation and lipid biosynthesis. PEX1 and PEX6 are hexameric AAA-type ATPases and both are necessary for the import of more than 50 peroxisomal resident proteins from the cytosol into peroxisomes. In this study, PEX1 N-terminal domain crystals have been prepared. The crystals belong to space group P3(1) or P3(2), with unit-cell parameters a = b = 63.5 A, c = 33.5 A, and contain one protein molecule per crystallographic asymmetric unit. An intensity data set was collected to a resolution of 2.05 A.
authors.affiliation: Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Kumiko
authors.initials: K
authors.lastname: Shiozawa
authors.forename: Nobuo
authors.initials: N
authors.lastname: Maita
authors.forename: Kentaro
authors.initials: K
authors.lastname: Tomii
authors.forename: Azusa
authors.initials: A
authors.lastname: Seto
authors.forename: Natsuko
authors.initials: N
authors.lastname: Goda
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Akiyama
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Shimizu
authors.forename: Masahiro
authors.initials: M
authors.lastname: Shirakawa
authors.forename: Hidekazu
authors.initials: H
authors.lastname: Hiroaki
mesh_terms: D000074183:ATPases Associated with Diverse Cellular Activities; D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary
chemical_list: D010446:Peptide Fragments; D000251:Adenosine Triphosphatases; D000074183:ATPases Associated with Diverse Cellular Activities; C495989:Pex1 protein, mouse