PDBsum entry: 1hjp

DNA recombination

PDB id: 1hjp

Contents

Protein chain

186 a.a. *

Waters ×19

* Residue conservation analysis

PDB id:

1hjp

Name:

DNA recombination

Title:

Holliday junction binding protein ruva from e. Coli

Structure:

Ruva. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Cell_line: bl21. Gene: ruva. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Homo-Tetramer (from PDB file)

Resolution:

2.50Å R-factor: 0.229 R-free: 0.294

Authors:

T.Nishino,M.Ariyoshi,H.Iwasaki,H.Shinagawa,K.Morikawa

Key ref:

T.Nishino et al. (1998). Functional analyses of the domain structure in the Holliday junction binding protein RuvA. Structure, 6, 11-21. PubMed id: 9493263

Date:

21-Aug-97 Release date: 25-Feb-98

Protein chain

P0A809  (RUVA_ECOLI) -  Holliday junction ATP-dependent DNA helicase RuvA

Seq: 203 a.a.

Struc: 186 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.4.12 - Dna helicase.
• Reaction: ATP + H₂O = ADP + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: Holliday junction helicase complex (1 term)
• Biological process: response to DNA damage stimulus (4 terms)
• Biochemical function: nucleotide binding (7 terms)

reference

Structure 6:11-21 (1998)

PubMed id: 9493263

Functional analyses of the domain structure in the Holliday junction binding protein RuvA.

T.Nishino, M.Ariyoshi, H.Iwasaki, H.Shinagawa, K.Morikawa.

ABSTRACT

BACKGROUND: Homologous recombination is crucial for genetic diversity and repairing damaged chromosomes. In Escherichia coli cells, the RuvA, RuvB and RuvC proteins participate in the processing of an important intermediate, the Holliday junction. The RuvA-RuvB protein complex facilitates branch migration of the junction, depending on ATP hydrolysis. The atomic structure of RuvA should enable critical questions to be addressed about its specific interactions with the Holliday junction and the RuvB protein. RESULTS: The crystal structure of RuvA shows the tetrameric molecules with a fourfold axis at the center. Each subunit consists of three distinct domains, some of which contain important secondary structure elements for DNA binding. Together with the detailed structural information, the biochemical assays of various mutant RuvA proteins and domains, isolated by partial proteolysis, allowed us to define the functional roles of these domains in Holliday junction binding and the RuvB interaction. CONCLUSIONS: The RuvA molecule is formed by four identical subunits, each with three domains, I, II and III. The locations of the putative DNA-binding motifs define an interface between the DNA and the Holliday junction. Domain III is weakly attached to the core region, comprising domains I and II; the core domains can form a tetramer in the absence of domain III. Functional analyses of the mutant proteins and the partial digestion products, including Holliday junction binding and branch-migration assays, revealed that domain III and the preceding loop are crucial for RuvB binding and branch migration, although this region is not required for the junction-DNA binding.