1ako

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{{STRUCTURE_1ako| PDB=1ako | SCENE= }}
{{STRUCTURE_1ako| PDB=1ako | SCENE= }}
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'''EXONUCLEASE III FROM ESCHERICHIA COLI'''
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===EXONUCLEASE III FROM ESCHERICHIA COLI===
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==Overview==
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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'--&gt;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 the alpha beta-sandwich, in a region dominated by positive electrostatic potential. Residues conserved among AP endonucleases from bacteria to man cluster within this active site and appear to participate in phosphate-bond cleavage at AP sites through a nucleophilic attack facilitated by a single bound metal ion.
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{{ABSTRACT_PUBMED_7885481}}
==About this Structure==
==About this Structure==
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[[Category: Exonuclease]]
[[Category: Exonuclease]]
[[Category: Nuclease]]
[[Category: Nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:23:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:02:49 2008''

Revision as of 14:02, 30 June 2008

Image:1ako.png

Template:STRUCTURE 1ako

EXONUCLEASE III FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 7885481

About this Structure

1AKO is a Single protein structure of sequence from Escherichia coli. 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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