1nlt

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The crystal structure of Hsp40 Ydj1

Structural highlights

1nlt is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAS5_YEAST Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The mechanisms by which Hsp40 functions as a molecular chaperone to recognize and bind non-native polypeptides is not understood. We have identified a peptide substrate for Ydj1, a member of the type I Hsp40 from yeast. The structure of the Ydj1 peptide binding fragment and its peptide substrate complex was determined to 2.7 A resolution. The complex structure reveals that Ydj1 peptide binding fragment forms an L-shaped molecule constituted by three domains. The domain I exhibits a similar protein folds as domain III while the domain II contains two Zinc finger motifs. The peptide substrate binds Ydj1 by forming an extra beta strand with domain I of Ydj1. The Leucine residue in the middle of the peptide substrate GWLYEIS inserts its side chain into a hydrophobic pocket formed on the molecular surface of Ydj1 domain I. The Zinc finger motifs located in the Ydj1 domain II are not in the vicinity of peptide substrate binding site.

The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate.,Li J, Qian X, Sha B Structure. 2003 Dec;11(12):1475-83. PMID:14656432[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
24 reviews cite this structure
The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
Kampinga et al. (2010)
23 more
65 other articles
No citations found

References

  1. ↑ Hon T, Lee HC, Hach A, Johnson JL, Craig EA, Erdjument-Bromage H, Tempst P, Zhang L. The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol. 2001 Dec;21(23):7923-32. PMID:11689685 doi:10.1128/MCB.21.23.7923-7932.2001
  2. ↑ Li J, Qian X, Sha B. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure. 2003 Dec;11(12):1475-83. PMID:14656432

Contents


PDB ID 1nlt

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