1EXK
SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.
Summary for 1EXK
| Entry DOI | 10.2210/pdb1exk/pdb |
| NMR Information | BMRB: 4677 |
| Descriptor | DNAJ PROTEIN, ZINC ION (2 entities in total) |
| Functional Keywords | extended beta-hairpin, cxxcxgxg, zinc-binding motif, chaperone |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P08622 |
| Total number of polymer chains | 1 |
| Total formula weight | 8661.52 |
| Authors | Martinez-Yamout, M.,Legge, G.B.,Zhang, O.,Wright, P.E.,Dyson, H.J. (deposition date: 2000-05-03, release date: 2000-07-26, Last modification date: 2024-05-22) |
| Primary citation | Martinez-Yamout, M.,Legge, G.B.,Zhang, O.,Wright, P.E.,Dyson, H.J. Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J.Mol.Biol., 300:805-818, 2000 Cited by PubMed Abstract: The solution structure of the cysteine-rich (CR) domain of Escherichia coli DnaJ has been solved by NMR methods. The structure of a 79 residue CR domain construct shows a novel fold with an overall V-shaped extended beta-hairpin topology. The CR domain is characterized by four C-X-X-C-X-G-X-G sequence motifs that bind two zinc ions. Residues in these two zinc modules show strong similarities in the grouping of resonances in the (15)N-(1)H HSQC spectrum and display pseudo-symmetry of the motifs in the calculated structures. The conformation of the cysteine residues coordinated to the zinc ion resembles that of the rubredoxin-knuckle, but there are significant differences in hydrogen bonding patterns in the two motifs. Zinc (15)N-(1)H HSQC titrations indicate that the fold of the isolated DnaJ CR domain is zinc-dependent and that one zinc module folds before the other. The C-X-X-C-X-G-X-G sequence motif is highly conserved in CR domains from a wide variety of species. The three-dimensional structure of the E. coli CR domain indicates that this sequence conservation is likely to result in a conserved structural motif. PubMed: 10891270DOI: 10.1006/jmbi.2000.3923 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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