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[[Image:1ako.gif|left|200px]]


{{Structure
==EXONUCLEASE III FROM ESCHERICHIA COLI==
|PDB= 1ako |SIZE=350|CAPTION= <scene name='initialview01'>1ako</scene>, resolution 1.7&Aring;
<StructureSection load='1ako' size='340' side='right'caption='[[1ako]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE= <scene name='pdbsite=MG1:Mg+Binding+Site'>MG1</scene>
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1ako]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AKO FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE= XTH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ako FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ako OCA], [https://pdbe.org/1ako PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ako RCSB], [https://www.ebi.ac.uk/pdbsum/1ako PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ako ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/EX3_ECOLI EX3_ECOLI] Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ak/1ako_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ako ConSurf].
<div style="clear:both"></div>


'''EXONUCLEASE III FROM ESCHERICHIA COLI'''
==See Also==
 
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
 
*[[Exonuclease 3D structures|Exonuclease 3D structures]]
==Overview==
__TOC__
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.
</StructureSection>
 
[[Category: Escherichia coli K-12]]
==About this Structure==
[[Category: Large Structures]]
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].
[[Category: Cunningham RP]]
 
[[Category: Kuo C-F]]
==Reference==
[[Category: Mol CD]]
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: Tainer JA]]
[[Category: Escherichia coli]]
[[Category: Thayer MM]]
[[Category: Exodeoxyribonuclease III]]
[[Category: Single protein]]
[[Category: Cunningham, R P.]]
[[Category: Kuo, C F.]]
[[Category: Mol, C D.]]
[[Category: Tainer, J A.]]
[[Category: Thayer, M M.]]
[[Category: ap-endonuclease]]
[[Category: dna repair]]
[[Category: exonuclease]]
[[Category: nuclease]]
 
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Retrieved from "https://proteopedia.org/1ako"