1ako

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[[Image:1ako.gif|left|200px]]<br /><applet load="1ako" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ako.gif|left|200px]]
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caption="1ako, resolution 1.7&Aring;" />
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'''EXONUCLEASE III FROM ESCHERICHIA COLI'''<br />
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{{Structure
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|PDB= 1ako |SIZE=350|CAPTION= <scene name='initialview01'>1ako</scene>, resolution 1.7&Aring;
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|SITE= <scene name='pdbsite=MG1:Mg+Binding+Site'>MG1</scene>
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|LIGAND=
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|ACTIVITY= [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]
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|GENE= XTH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''EXONUCLEASE III FROM ESCHERICHIA COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKO OCA].
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1AKO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKO OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7885481 7885481]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7885481 7885481]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Exodeoxyribonuclease III]]
[[Category: Exodeoxyribonuclease III]]
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[[Category: nuclease]]
[[Category: nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:58:56 2008''

Revision as of 07:58, 20 March 2008


PDB ID 1ako

Drag the structure with the mouse to rotate
, resolution 1.7Å
Sites:
Gene: XTH (Escherichia coli)
Activity: Exodeoxyribonuclease III, with EC number 3.1.11.2
Coordinates: save as pdb, mmCIF, xml



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. 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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