title: Atomic structure of a pyrimidine-dimer specific excision-repair enzyme from bacteriophage T4.
abstract: T4 endonuclease V is an enzyme responsible for the first step of a pyrimidine-dimer specific excision-repair process. The three-dimensional structure of this enzyme has been determined at 1.6A resolution by X-ray crystallography. The enzyme consists of one single compact domain classified into the all alpha structure. This single domain possesses two distinct catalytic activities, a pyrimidine-dimer glycosylase and an apurinic/apyrimidinic endonuclease. The backbone of the enzyme represents a unique folding scheme incompatible with close packing of alpha-helices. The refined structure suggests possible residues that participate in interactions with DNA.
authors.affiliation: Protein Engineering Research Institute, Osaka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Morikawa
authors.forename: O
authors.initials: O
authors.lastname: Matsumoto
authors.forename: M
authors.initials: M
authors.lastname: Tsujimoto
authors.forename: K
authors.initials: K
authors.lastname: Katayanagi
authors.forename: T
authors.initials: T
authors.lastname: Doi
authors.forename: M
authors.initials: M
authors.lastname: Ariyoshi
authors.forename: M
authors.initials: M
authors.lastname: Ikehara
authors.forename: T
authors.initials: T
authors.lastname: Inaoka
authors.forename: E
authors.initials: E
authors.lastname: Ohtsuka
mesh_terms: D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000201:enzymology*; D043224:Deoxyribonuclease (Pyrimidine Dimer); D004706:Endodeoxyribonucleases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011740:Pyrimidine Dimers / Q000378:metabolism*; D014764:Viral Proteins; D014961:X-Ray Diffraction
chemical_list: D011740:Pyrimidine Dimers; D014764:Viral Proteins; D004706:Endodeoxyribonucleases; C470698:endonuclease V, phage T4; D043224:Deoxyribonuclease (Pyrimidine Dimer)