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2JC5

Apurinic Apyrimidinic (AP) endonuclease (NApe) from Neisseria Meningitidis

Summary for 2JC5
Entry DOI10.2210/pdb2jc5/pdb
Related2JC4
DescriptorEXODEOXYRIBONUCLEASE, MAGNESIUM ION, BICINE, ... (6 entities in total)
Functional Keywordshydrolase, neisseria meningitidis, repair phosphodiesterase, dna repair, exonuclease, endonuclease
Biological sourceNEISSERIA MENINGITIDIS
Total number of polymer chains1
Total formula weight30247.47
Authors
Carpenter, E.P.,Corbett, A.,Thomson, H.,Adacha, J.,Jensen, K.,Bergeron, J.,Kasampalidis, I.,Exley, R.,Winterbotham, M.,Tang, C.,Baldwin, G.S.,Freemont, P. (deposition date: 2006-12-19, release date: 2007-03-06, Last modification date: 2023-12-13)
Primary citationCarpenter, E.P.,Corbett, A.,Thomson, H.,Adacha, J.,Jensen, K.,Bergeron, J.,Kasampalidis, I.,Exley, R.,Winterbotham, M.,Tang, C.,Baldwin, G.S.,Freemont, P.
Ap Endonuclease Paralogues with Distinct Activities in DNA Repair and Bacterial Pathogenesis.
Embo J., 26:1363-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17318183
DOI: 10.1038/SJ.EMBOJ.7601593
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

237735

数据于2025-06-18公开中

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