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==3'-5' exonuclease (NExo) from Neisseria Meningitidis== | |||
<StructureSection load='2jc4' size='340' side='right'caption='[[2jc4]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jc4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JC4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jc4 OCA], [https://pdbe.org/2jc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jc4 RCSB], [https://www.ebi.ac.uk/pdbsum/2jc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jc4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9K100_NEIMB Q9K100_NEIMB] | |||
== 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/jc/2jc4_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2jc4 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Oxidative stress is a principal cause of DNA damage, and mechanisms to repair this damage are among the most highly conserved of biological processes. Oxidative stress is also used by phagocytes to attack bacterial pathogens in defence of the host. We have identified and characterised two apurinic/apyrimidinic (AP) endonuclease paralogues in the human pathogen Neisseria meningitidis. The presence of multiple versions of DNA repair enzymes in a single organism is usually thought to reflect redundancy in activities that are essential for cellular viability. We demonstrate here that these two AP endonuclease paralogues have distinct activities in DNA repair: one is a typical Neisserial AP endonuclease (NApe), whereas the other is a specialised 3'-phosphodiesterase Neisserial exonuclease (NExo). The lack of AP endonuclease activity of NExo is shown to be attributable to the presence of a histidine side chain, blocking the abasic ribose-binding site. Both enzymes are necessary for survival of N. meningitidis under oxidative stress and during bloodstream infection. The novel functional pairing of NExo and NApe is widespread among bacteria and appears to have evolved independently on several occasions. | |||
AP endonuclease paralogues with distinct activities in DNA repair and bacterial pathogenesis.,Carpenter EP, Corbett A, Thomson H, Adacha J, Jensen K, Bergeron J, Kasampalidis I, Exley R, Winterbotham M, Tang C, Baldwin GS, Freemont P EMBO J. 2007 Mar 7;26(5):1363-72. Epub 2007 Feb 22. PMID:17318183<ref>PMID:17318183</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jc4" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Exonuclease 3D structures|Exonuclease 3D structures]] | |||
[[Category: | == References == | ||
[[Category: Adacha | <references/> | ||
[[Category: Baldwin | __TOC__ | ||
[[Category: Bergeron | </StructureSection> | ||
[[Category: Carpenter | [[Category: Large Structures]] | ||
[[Category: Corbett | [[Category: Neisseria meningitidis]] | ||
[[Category: Exley | [[Category: Adacha J]] | ||
[[Category: Freemont | [[Category: Baldwin G]] | ||
[[Category: Jensen | [[Category: Bergeron J]] | ||
[[Category: Kasampalidis | [[Category: Carpenter EP]] | ||
[[Category: Tang | [[Category: Corbett A]] | ||
[[Category: Thomson | [[Category: Exley R]] | ||
[[Category: Winterbotham | [[Category: Freemont P]] | ||
[[Category: Jensen K]] | |||
[[Category: Kasampalidis I]] | |||
[[Category: Tang C]] | |||
[[Category: Thomson H]] | |||
[[Category: Winterbotham M]] | |||
Latest revision as of 08:18, 17 October 2024
3'-5' exonuclease (NExo) from Neisseria Meningitidis3'-5' exonuclease (NExo) from Neisseria Meningitidis
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 PubMedOxidative stress is a principal cause of DNA damage, and mechanisms to repair this damage are among the most highly conserved of biological processes. Oxidative stress is also used by phagocytes to attack bacterial pathogens in defence of the host. We have identified and characterised two apurinic/apyrimidinic (AP) endonuclease paralogues in the human pathogen Neisseria meningitidis. The presence of multiple versions of DNA repair enzymes in a single organism is usually thought to reflect redundancy in activities that are essential for cellular viability. We demonstrate here that these two AP endonuclease paralogues have distinct activities in DNA repair: one is a typical Neisserial AP endonuclease (NApe), whereas the other is a specialised 3'-phosphodiesterase Neisserial exonuclease (NExo). The lack of AP endonuclease activity of NExo is shown to be attributable to the presence of a histidine side chain, blocking the abasic ribose-binding site. Both enzymes are necessary for survival of N. meningitidis under oxidative stress and during bloodstream infection. The novel functional pairing of NExo and NApe is widespread among bacteria and appears to have evolved independently on several occasions. AP endonuclease paralogues with distinct activities in DNA repair and bacterial pathogenesis.,Carpenter EP, Corbett A, Thomson H, Adacha J, Jensen K, Bergeron J, Kasampalidis I, Exley R, Winterbotham M, Tang C, Baldwin GS, Freemont P EMBO J. 2007 Mar 7;26(5):1363-72. Epub 2007 Feb 22. PMID:17318183[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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