Preliminary X-ray crystallographic studies of yeast Hsp40 Ydj1 complexed with its peptide substrate.
The mechanism by which Hsp40 functions as a molecular chaperone, recognizing and binding non-native polypeptides, is not understood. To investigate the mechanism, the yeast type I Hsp40 protein Ydj1 C-terminal peptide-binding fragment has been crystallized complexed with its peptide substrate. The crystals diffract to 2.70 A using a synchrotron X-ray source and belong to space group P3(2)21 or P3(1)21, with unit-cell parameters a = b = 55.21, c = 161.87 A, alpha = beta = 90, gamma = 120 degrees. There is one Ydj1 peptide-binding fragment and one peptide substrate in the asymmetric unit, which corresponds to a solvent content of approximately 42%. Structure determination by MAD methods is under way.
Li
Jingzhi
J
Department of Cell Biology, Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, USA.
Sha
Bingdong
B
D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry*; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D018832:Molecular Chaperones / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding
D005656:Fungal Proteins; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010455:Peptides