PDBsum entry: 1hdj

Molecular chaperone

PDB id: 1hdj

Contents

Protein chain

77 a.a. *

* Residue conservation analysis

PDB id:

1hdj

Name:

Molecular chaperone

Title:

Human hsp40 (hdj-1), nmr

Structure:

Human hsp40. Chain: a. Fragment: j-domain. Synonym: hdj-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

Y.Q.Qian,D.Patel,F.-U.Hartl,D.J.Mccoll

Key ref:

Y.Q.Qian et al. (1996). Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J Mol Biol, 260, 224-235. PubMed id: 8764402 DOI: 10.1006/jmbi.1996.0394

Date:

09-May-96 Release date: 08-Nov-96

Protein chain

P25685  (DNJB1_HUMAN) -  DnaJ homolog subfamily B member 1

Seq: 340 a.a.

Struc: 77 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: protein folding (1 term)
• Biochemical function: heat shock protein binding (2 terms)

DOI no: 10.1006/jmbi.1996.0394

J Mol Biol 260:224-235 (1996)

PubMed id: 8764402

Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.

Y.Q.Qian, D.Patel, F.U.Hartl, D.J.McColl.

ABSTRACT

The J-domain is a highly conserved domain found in all members of the DnaJ family of molecular chaperones. The three-dimensional structure of a recombinant, uniformly 15N-labeled 77-residue polypeptide containing the complete J-domain from human Hsp40 (HDJ-1) has been determined by nuclear magnetic resonance (NMR) spectroscopy in solution. On the basis of 876 upper distance constraints derived from nuclear Overhauser effects (NOE) and 173 dihedral angle constraints, a group of 20 conformers representing the solution structure of the HDJ-1 J-domain was computed with the program DIANA and energy-minimized with the program OPAL. The average of the pairwise root-mean-square deviations of the individual NMR conformers relative to the mean coordinates for the backbone atoms N, C2 and C' of residues 4 to 54 and 4 to to 66 is 0.88 and 0.99 A respectively. The molecular architecture includes four helices composed of residues 5 to 9, 15 to 28, 40 to 54 and 60 to 66. A turn composed of residues 10 to 14 links helices I and II, and a loop composed of residues 29 to 39 containing a highly conserved tripeptide HPD (residues 31 to 33) connects the antiparallel helices II and III. The tertiary fold formed by helix I-turn-helix II-loop-helix III forms a closed structural core; the less defined helix IV stands away from the core of the domain. The side-chains of the tripeptide HPD extend out from the core of the structure in the opposite direction from helix IV. The structure supports the hypothesis that the highly conserved tripeptide could play a key role in the interaction of Hsp40 with the molecular chaperone, Hsp70.

Selected figure(s)

Figure 4.
Figure 4. Stereo view of the polypeptide backbone atoms N, C a and C' for the 20 energy-refined DIANA conformers of the HDJ-1 J-domain. The superposition was taken for best fit of the backbone atoms N, C a and C' of residues 4 to 54. The color coding is: residues 0 to 3, 10 to 14, green; 4 to 9 (helix I), white; 15 to 28 (helix II), magenta; 40 to 54 (helix III), yellow; 60 to 66 (helix IV), orange; 29 to 39, 55 to 59 and 67 to 76, cyan.

Figure 7.
Figure 7. Ribbon drawing of one energy refined DIANA conformer of the HDJ-1 J-domain (residues 0 to 76). The chain termini are identified by the letters N and C. Helices I to IV are shown in cyan, the loop and turns connecting the helices are shown in orange. The HPD tripeptide is indicated by the residues in red (His31), green (Pro32) and blue (Asp33). Six highly conserved residues (positions 19, 27, 44, 50, 51 and 54) involved in the stabilization of the structural core of the J-domain are indicated in yellow.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1996, 260, 224-235) copyright 1996.

Figures were selected by an automated process.