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SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.

Overview

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.

About this Structure

1EXK is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ., Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ, J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:10891270

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