Atomic structure of a pyrimidine-dimer specific excision-repair enzyme from bacteriophage T4.
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.
Morikawa
K
K
Protein Engineering Research Institute, Osaka, Japan.
Matsumoto
O
O
Tsujimoto
M
M
Katayanagi
K
K
Doi
T
T
Ariyoshi
M
M
Ikehara
M
M
Inaoka
T
T
Ohtsuka
E
E
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
D011740:Pyrimidine Dimers; D014764:Viral Proteins; D004706:Endodeoxyribonucleases; C470698:endonuclease V, phage T4; D043224:Deoxyribonuclease (Pyrimidine Dimer)