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J Mol Biol. 1998 Apr 24;278(1):105-16.

Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the holliday junction.

Author information

1
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, Western Bank, S10 2TN, UK.

Abstract

Comparison of the structure of Escherichia coli RuvA with other proteins in the Protein Data Bank gives insights into the probable modes of association of RuvA with the Holliday junction during homologous recombination. All three domains of the RuvA protein possess striking structural similarities to other DNA-binding proteins. Additionally, the second domain of RuvA contains two copies of the helix-hairpin-helix (HhH) structural motif, which has been implicated in non-sequence-specific DNA binding. The two copies of the motif are related by approximate 2-fold symmetry and may form a bidentate DNA-binding module. The results described provide support for the organization of the arms of the DNA in our RuvA/Holliday junction complex model and support the involvement of the HhH motifs in DNA binding.

PMID:
9571037
DOI:
10.1006/jmbi.1998.1697
[Indexed for MEDLINE]

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