Crystallographic characterization of the N-terminal domain of PEX1.
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.
Shiozawa
Kumiko
K
Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Maita
Nobuo
N
Tomii
Kentaro
K
Seto
Azusa
A
Goda
Natsuko
N
Akiyama
Yutaka
Y
Shimizu
Toshiyuki
T
Shirakawa
Masahiro
M
Hiroaki
Hidekazu
H
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
D010446:Peptide Fragments; D000251:Adenosine Triphosphatases; D000074183:ATPases Associated with Diverse Cellular Activities; C495989:Pex1 protein, mouse