Crystal structure of the Holliday junction resolving enzyme T7 endonuclease I.

JM Hadden, MA Convery, AC Déclais, DM Lilley, S E V Phillips (Lead / Corresponding author)

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

We have solved the crystal structure of the Holliday junction resolving enzyme T7 endonuclease I at 2.1 A resolution using the multiwavelength anomalous dispersion (MAD) technique. Endonuclease I exhibits strong structural specificity for four-way DNA junctions. The structure shows that it forms a symmetric homodimer arranged in two well-separated domains. Each domain, however, is composed of elements from both subunits, and amino acid side chains from both protomers contribute to the active site. While no significant structural similarity could be detected with any other junction resolving enzyme, the active site is similar to that found in several restriction endonucleases. T7 endonuclease I therefore represents the first crystal structure of a junction resolving enzyme that is a member of the nuclease superfamily of enzymes.
Original languageEnglish
Pages (from-to)62-67
JournalNature Structural and Molecular Biology
Volume8
Issue number1
DOIs
Publication statusPublished - Jan 2001

Fingerprint Dive into the research topics of 'Crystal structure of the Holliday junction resolving enzyme T7 endonuclease I.'. Together they form a unique fingerprint.

  • Cite this