Crystal structure of T4 endonuclease VII resolving a Holliday junction

Christian Biertümpfel, Wei Yang () and Dietrich Suck ()
Additional contact information
Christian Biertümpfel: National Institute of Diabetes and Digestive and Kidney Diseases, Laboratory of Molecular Biology, 9000 Rockville Pike, Bethesda, Maryland 20892, USA
Wei Yang: National Institute of Diabetes and Digestive and Kidney Diseases, Laboratory of Molecular Biology, 9000 Rockville Pike, Bethesda, Maryland 20892, USA
Dietrich Suck: European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstr. 1, 69117 Heidelberg, Germany

Nature, 2007, vol. 449, issue 7162, 616-620

Abstract: Holliday reading Genetic recombination between homologous DNA duplexes plays a critical role in the maintenance and propagation of genomes. The central intermediate of the process is the four-way (Holliday) junction that links two DNA duplexes. This is ultimately resolved to form two separate DNA duplexes. Junction resolvases of various types are found in prokaryotes, eukaryotes and their viruses. These nucleases are highly selective for the structure of the DNA branchpoint. Two groups now describe crystal structures of complexes of two different junction-resolving enzymes, endonuclease 1 (phage T7) and endonuclease VII (phage T4), each bound to DNA junctions. Both enzymes significantly distort the structure of the junction on binding. The new structures reveal how the enzymes are selective for DNA junctions, as well as the principles of the cleavage reaction.

Date: 2007
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature06152 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:449:y:2007:i:7162:d:10.1038_nature06152

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature06152

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().