1ako
From Proteopedia
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| - | [[Image:1ako.gif|left|200px]]<br /> | + | [[Image:1ako.gif|left|200px]]<br /><applet load="1ako" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ako" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ako, resolution 1.7Å" /> | caption="1ako, resolution 1.7Å" /> | ||
'''EXONUCLEASE III FROM ESCHERICHIA COLI'''<br /> | '''EXONUCLEASE III FROM ESCHERICHIA COLI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] | + | 1AKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] Known structural/functional Site: <scene name='pdbsite=MG1:Mg Binding Site'>MG1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AKO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nuclease]] | [[Category: nuclease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:16:43 2007'' |
Revision as of 12:06, 18 December 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, 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.
About this Structure
1AKO is a Single protein structure of sequence from Escherichia coli. Active as Exodeoxyribonuclease III, with EC number 3.1.11.2 Known structural/functional Site: . 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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