2j63: Difference between revisions
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<StructureSection load='2j63' size='340' side='right'caption='[[2j63]], [[Resolution|resolution]] 2.48Å' scene=''> | <StructureSection load='2j63' size='340' side='right'caption='[[2j63]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j63]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2j63]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J63 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j63 OCA], [https://pdbe.org/2j63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j63 RCSB], [https://www.ebi.ac.uk/pdbsum/2j63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j63 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O15922_LEIMA O15922_LEIMA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Apurinic/apyrimidinic endonuclease 3D structures|Apurinic/apyrimidinic endonuclease 3D structures]] | *[[Apurinic/apyrimidinic endonuclease 3D structures|Apurinic/apyrimidinic endonuclease 3D structures]] | ||
*[[Endonuclease|Endonuclease]] | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leishmania major]] | ||
[[Category: Castillo-Acosta | [[Category: Castillo-Acosta VM]] | ||
[[Category: Gallego | [[Category: Gallego C]] | ||
[[Category: Gonzalez-Pacanowska | [[Category: Gonzalez-Pacanowska D]] | ||
[[Category: Harkiolaki | [[Category: Harkiolaki M]] | ||
[[Category: Ruiz-Perez | [[Category: Ruiz-Perez LM]] | ||
[[Category: Vidal | [[Category: Vidal AE]] | ||
[[Category: Wilson | [[Category: Wilson KS]] | ||
Latest revision as of 17:36, 13 December 2023
Crystal structure of AP endonuclease LMAP from Leishmania majorCrystal structure of AP endonuclease LMAP from Leishmania major
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedApurinic/apyrimidinic endonucleases initiate the repair of abasic sites produced either spontaneously, from attack of bases by reactive oxygen species or as intermediates during base excision repair. The catalytic properties and crystal structure of Leishmania major apurinic/apyrimidinic endonuclease are described and compared with those of human APE1 and bacterial exonuclease III. The purified enzyme is shown to possess apurinic/apyrimidinic endonuclease activity of the same order as eukaryotic and prokaryotic counterparts and an equally robust 3'-phosphodiesterase activity. Consistent with this, expression of the L. major endonuclease confers resistance to both methyl methane sulphonate and H2O2 in Escherichia coli repair-deficient mutants while expression of the human homologue only reverts methyl methane sulphonate sensitivity. Structural analyses and modelling of the enzyme-DNA complex demonstrates a high degree of conservation to previously characterized homologues, although subtle differences in the active site geometry might account for the high 3'-phosphodiesterase activity. Our results confirm that the L. major's enzyme is a key element in mediating repair of apurinic/apyrimidinic sites and 3'-blocked termini and therefore must play an important role in the survival of kinetoplastid parasites after exposure to the highly oxidative environment within the host macrophage. Crystal structure and DNA repair activities of the AP endonuclease from Leishmania major.,Vidal AE, Harkiolaki M, Gallego C, Castillo-Acosta VM, Ruiz-Perez LM, Wilson K, Gonzalez-Pacanowska D J Mol Biol. 2007 Nov 2;373(4):827-38. Epub 2007 Aug 19. PMID:17870086[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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