Purification, crystallization and preliminary X-ray crystallographic analysis of the human heat-shock protein 40 Hdj1 and its C-terminal peptide-binding domain.
Hsp40 is a co-chaperone of Hsp70 that correctly folds polypeptides that exist in non-native forms. The C-terminal peptide-binding domain (CTD) of the human Hsp40 Hdj1 has been purified and crystallized. In the presence of the C-terminal octapeptide of human Hsp70, four types of crystals, types I-B, II, III and IV, were grown and diffracted to 1.85, 2.51, 2.10 and 2.80 Å resolution, respectively. In the absence of the octapeptide, type I-A crystals of the CTD were grown that diffracted to 2.05 Å resolution. The full-length Hdj1 was also purified and crystallized (type V crystals); the crystal diffracted to 3.90 Å resolution.
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Hironori
H
Suzuki
Shuji
S
Noguchi
Hiroshi
H
Arakawa
Tadaaki
T
Tokida
Mariko
M
Hashimoto
Yoshinori
Y
Satow
D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D006801:Humans; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
C494647:DNAJB1 protein, human; D050956:HSP40 Heat-Shock Proteins; D010455:Peptides