1. The Crystal Structure of the C-terminal Fragment of Yeast Hsp40 Ydj1 Reveals Novel Dimerization Motif for Hsp40
- Author
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Wu, Yunkun, Li, Jingzhi, Jin, Zhongmin, Fu, Zhengqing, and Sha, Bingdong
- Subjects
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PROTEINS , *LEAVENING agents , *YEAST , *DIMERS - Abstract
The molecular chaperone Hsp40 functions as a dimer. The dimer formation is critical for Hsp40 molecular chaperone activity to facilitate Hsp70 to refold non-native polypeptides. We have determined the crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 that is responsible for Ydj1 dimerization by MAD method. The C-terminal fragment of Ydj1 comprises of the domain III of Ydj1 and the Ydj1 C-terminal dimerization motif. The crystal structure indicates that the dimerization motif of type I Hsp40 Ydj1 differs significantly from that of yeast type II Hsp40. The C terminus of type I Hsp40 Ydj1 from one monomer forms β-strands with the domain III from the other monomer in the homo-dimer. The L372 from Ydj1 C terminus inserts its side-chain into a hydrophobic pocket on domain III. The modeled full-length Ydj1 dimer structure reveals that a large cleft is formed between the two monomers. The domain IIs of Ydj1 monomers that contain the zinc-finger motifs points directly against each other. [Copyright &y& Elsevier]
- Published
- 2005
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