1XAO

Hsp40-Ydj1 dimerization domain

Summary for 1XAO

• Entry DOI: 10.2210/pdb1xao/pdb
• Related: 1C3G 1NLT
• Descriptor: Mitochondrial protein import protein MAS5 (2 entities in total)
• Functional Keywords: beta sheets, chaperone
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P25491
• Total number of polymer chains: 2
• Total formula weight: 26532.64

Authors

Wu, Y.,Sha, B. (deposition date: 2004-08-26, release date: 2005-05-03, Last modification date: 2024-02-14)

Primary citation

Wu, Y.,Li, J.,Jin, Z.,Fu, Z.,Sha, B.
The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40
J.Mol.Biol., 346:1005-1011, 2005

PubMed 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 beta-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.

PubMed: 15701512
DOI: 10.1016/j.jmb.2004.12.040

Experimental method

X-RAY DIFFRACTION (2.07 Å)