1ako
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(New page: 200px<br /> <applet load="1ako" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ako, resolution 1.7Å" /> '''EXONUCLEASE III FROM...)
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Revision as of 17:20, 29 October 2007
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EXONUCLEASE III FROM ESCHERICHIA COLI
Overview
The repair of DNA requires the removal of abasic sites, which are, constantly generated in vivo both spontaneously and by enzymatic removal, of uracil, and of bases damaged by active oxygen species, alkylating, agents and ionizing radiation. The major apurinic/apyrimidinic (AP), DNA-repair endonuclease in Escherichia coli is the multifunctional enzyme, exonuclease III, which also exhibits 3'-repair diesterase, 3'-->5', exonuclease, 3'-phosphomonoesterase and ribonuclease activities. We report, here the 1.7 A resolution crystal structure of exonuclease III which, reveals a 2-fold symmetric, four-layered alpha beta fold with similarities, to both deoxyribonuclease I and RNase H. In the ternary complex determined, at 2.6 A resolution, Mn2+ and dCMP bind to exonuclease III at one end of, ... [(full description)]
About this Structure
1AKO is a [Single protein] structure of sequence from [Escherichia coli]. Active as [[1]], with EC number [3.1.11.2]. Full crystallographic information is available from [OCA].
Reference
Structure and function of the multifunctional DNA-repair enzyme exonuclease III., Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA, Nature. 1995 Mar 23;374(6520):381-6. PMID:7885481
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