X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer.
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-alpha 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.
Morikawa
K
K
Protein Engineering Research Institute, Osaka, Japan.
Matsumoto
O
O
Tsujimoto
M
M
Katayanagi
K
K
Ariyoshi
M
M
Doi
T
T
Ikehara
M
M
Inaoka
T
T
Ohtsuka
E
E
D000595:Amino Acid Sequence; D004260:DNA Repair; D043224:Deoxyribonuclease (Pyrimidine Dimer); D004563:Electrochemistry; D004706:Endodeoxyribonucleases / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011740:Pyrimidine Dimers / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013604:T-Phages / Q000201:enzymology; D014764:Viral Proteins; D014961:X-Ray Diffraction
D011740:Pyrimidine Dimers; D014764:Viral Proteins; D004706:Endodeoxyribonucleases; C470698:endonuclease V, phage T4; D043224:Deoxyribonuclease (Pyrimidine Dimer)