1Q8R

Structure of E.coli RusA Holliday junction resolvase

Summary for 1Q8R

• Entry DOI: 10.2210/pdb1q8r/pdb
• Descriptor: Crossover junction endodeoxyribonuclease rusA (2 entities in total)
• Functional Keywords: extended mixed beta sheet, chorismate mutase-like fold, recombination, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 27735.87

Authors

Rafferty, J.B.,Bolt, E.L.,Muranova, T.A.,Sedelnikova, S.E.,Leonard, P.,Pasquo, A.,Baker, P.J.,Rice, D.W.,Sharples, G.J.,Lloyd, R.G. (deposition date: 2003-08-22, release date: 2004-01-06, Last modification date: 2024-02-14)

Primary citation

Rafferty, J.B.,Bolt, E.L.,Muranova, T.A.,Sedelnikova, S.E.,Leonard, P.,Pasquo, A.,Baker, P.J.,Rice, D.W.,Sharples, G.J.,Lloyd, R.G.
The structure of Escherichia coli RusA endonuclease reveals a new Holliday junction DNA binding fold
Structure, 11:1557-1567, 2003

PubMed Abstract: Holliday junction resolution performed by a variety of structure-specific endonucleases is a key step in DNA recombination and repair. It is believed that all resolvases carry out their reaction chemistries in a similar fashion, utilizing a divalent cation to facilitate the hydrolysis of the phosphodiester backbone of the DNA, but their architecture varies. To date, with the exception of bacteriophage T4 endonuclease VII, each of the known resolvase enzyme structures has been categorized into one of two families: the integrases and the nucleases. We have now determined the structure of the Escherichia coli RusA Holliday junction resolvase, which reveals a fourth structural class for these enzymes. The structure suggests that dimer formation is essential for Mg(2+) cation binding and hence catalysis and that like the other resolvases, RusA distorts its Holliday junction target upon binding. Key residues identified by mutagenesis experiments are well positioned to interact with the DNA.

PubMed: 14656440
DOI: 10.1016/j.str.2003.11.004

Experimental method

X-RAY DIFFRACTION (1.899 Å)