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Expression, purification, crystallization and X‐ray diffraction studies of the molecular chaperone prefoldin from Homo sapiens
Author(s) -
Aikawa Yoshiki,
Kida Hiroshi,
Nishitani Yuichi,
Miki Kunio
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15013990
Subject(s) - chaperone (clinical) , chaperonin , protein folding , recombinant dna , crystallization , biophysics , tubulin , homo sapiens , chemistry , biology , microbiology and biotechnology , crystallography , biochemistry , gene , microtubule , medicine , organic chemistry , pathology , sociology , anthropology
Proper protein folding is an essential process for all organisms. Prefoldin (PFD) is a molecular chaperone that assists protein folding by delivering non‐native proteins to group II chaperonin. A heterohexamer of eukaryotic PFD has been shown to specifically recognize and deliver non‐native actin and tubulin to chaperonin‐containing TCP‐1 (CCT), but the mechanism of specific recognition is still unclear. To determine its crystal structure, recombinant human PFD was reconstituted, purified and crystallized. X‐ray diffraction data were collected to 4.7 Å resolution. The crystals belonged to space group P 2 1 2 1 2, with unit‐cell parameters a = 123.2, b = 152.4, c = 105.9 Å.