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Science 24 April 1992:
Vol. 256. no. 5056, pp. 523 - 526
DOI: 10.1126/science.1575827
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Articles

Science, Vol 256, Issue 5056, 523-526
Copyright © 1992 by American Association for the Advancement of Science

articles

X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer

K Morikawa, O Matsumoto, M Tsujimoto, K Katayanagi, M Ariyoshi, T Doi, M Ikehara, T Inaoka, and E Ohtsuka

Protein Engineering Research Institute, Osaka, Japan.

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.


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