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PDBsum entry 4b5h
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Hydrolase/DNA
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PDB id
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4b5h
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References listed in PDB file
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Key reference
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Title
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Structural basis for the recognition and cleavage of abasic DNA in neisseria meningitidis.
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Authors
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D.Lu,
J.Silhan,
J.T.Macdonald,
E.P.Carpenter,
K.Jensen,
C.M.Tang,
G.S.Baldwin,
P.S.Freemont.
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Ref.
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Proc Natl Acad Sci U S A, 2012,
109,
16852-16857.
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PubMed id
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Abstract
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Base excision repair (BER) is a highly conserved DNA repair pathway throughout
all kingdoms from bacteria to humans. Whereas several enzymes are required to
complete the multistep repair process of damaged bases, apurinic-apyrimidic (AP)
endonucleases play an essential role in enabling the repair process by
recognizing intermediary abasic sites cleaving the phosphodiester backbone 5' to
the abasic site. Despite extensive study, there is no structure of a bacterial
AP endonuclease bound to substrate DNA. Furthermore, the structural mechanism
for AP-site cleavage is incomplete. Here we report a detailed structural and
biochemical study of the AP endonuclease from Neisseria meningitidis that has
allowed us to capture structural intermediates providing more complete snapshots
of the catalytic mechanism. Our data reveal subtle differences in AP-site
recognition and kinetics between the human and bacterial enzymes that may
reflect different evolutionary pressures.
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