| Literature DB >> 1575827 |
K Morikawa1, O Matsumoto, M Tsujimoto, K Katayanagi, M Ariyoshi, T Doi, M Ikehara, T Inaoka, E Ohtsuka.
Abstract
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.Entities:
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Year: 1992 PMID: 1575827 DOI: 10.1126/science.1575827
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728