1ako

<StructureSection load='1ako' size='340' side='right' caption='[[1ako]], [[Resolution|resolution]] 1.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ako]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AKO FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XTH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ako FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ako OCA], [http://pdbe.org/1ako PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ako RCSB], [http://www.ebi.ac.uk/pdbsum/1ako PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ak/1ako_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:7885481</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ako" style="background-color:#fffaf0;"></div>

*[[Endonuclease|Endonuclease]]

*[[Exonuclease|Exonuclease]]

[[Category: Ecoli]]

[[Category: Exodeoxyribonuclease III]]

[[Category: Cunningham, R P]]

[[Category: Kuo, C F]]

[[Category: Mol, C D]]

[[Category: Tainer, J A]]

[[Category: Thayer, M M]]

[[Category: Nuclease]]