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Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Martinez-Yamout M,Legge GB,Zhang O,Wright PE,Dyson HJ

doi

10.1006/jmbi.2000.3923

keywords:

subject

Has Abstract

pub_date

2000-07-21 00:00:00

pages

805-18

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)93923-8

journal_volume

300

pub_type

杂志文章

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