X-ray Structure of T4 Endonuclease V: An Excision Repair Enzyme Specific for a Pyrimidine Dimer

• Published in: Science (American Association for the Advancement of Science) Vol. 256; no. 5056; pp. 523 - 526
• Main Authors: Morikawa, K., Matsumoto, O., Tsujimoto, M., Katayanagi, K., Ariyoshi, M., Doi, T., Ikehara, M., Inaoka, T., Ohtsuka, E.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 24-04-1992; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Atoms; Biological and medical sciences; Crystal structure; Crystals; Deoxyribonuclease (Pyrimidine Dimer); DNA; DNA Repair; DNA restriction enzymes; Electrochemistry; Electrostatic bonding; Endodeoxyribonucleases - chemistry; Endodeoxyribonucleases - metabolism; Enzymes; Fundamental and applied biological sciences. Psychology; Genetic mutation; Glycosylation; Hydrogen Bonding; Inhalants; Molecular biophysics; Molecular interactions; Molecular Sequence Data; Molecular Structure; Molecules; Mutagenesis, Site-Directed; Personality; Protein Conformation; Protein structure; Proteins; Proximity; Pyrimidine dimers; Pyrimidine Dimers - metabolism; Restriction enzymes, DNA; Structure; Structure in molecular biology; Structure-Activity Relationship; Substrate Specificity; T-Phages - enzymology; Tridimensional structure; Viral Proteins; Water; X-ray crystallography; X-Ray Diffraction; Enzyme; Endodeoxyribonuclease V; Refinement; Binding site; X ray diffraction; Spatial structure; Myoviridae; Virus; Substrate; T even phage; Catalytic site; Phage; Phage T4; Crystalline structure
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1575827

The x-ray structure of T4 endonuclease V, an enzyme responsible for the first step of a pyrimidine-dimer-specific excision-repair pathway, was determined at a 1.6-angstrom resolution. The enzyme consists of a single compact domain classified into an all-α structure. This single domain has two distinct catalytic activities: it functions as a pyrimidine dimer glycosylase and as an apurinic-apyrimidinic endonuclease. The amino-terminal segment penetrates between two major helices and prevents their direct contact. The refined structure suggests the residues involved in the substrate binding and the catalysis of the glycosylation reaction.