1exk is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ. Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:10891270 doi:10.1006/jmbi.2000.3923
