PMID:10891270
| Citation |
Martinez-Yamout, M, Legge, GB, Zhang, O, Wright, PE and Dyson, HJ (2000) Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J. Mol. Biol. 300:805-18 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1006/jmbi.2000.3923 |
| Keywords |
Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Conserved Sequence; Cysteine/chemistry; Cysteine/metabolism; Escherichia coli/chemistry; Escherichia coli Proteins; HSP40 Heat-Shock Proteins; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptides/metabolism; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Solutions; Zinc/metabolism |
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