4b5h

Substate bound inactive mutant of Neisseria AP endonuclease in presence of metal ions

spinqualitylabelsall models 4b5h, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b5h is a 3 chain structure with sequence from Neisseria meningitidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.05Å Ligands: 3DR, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7DD47_NEIMB Publication Abstract from PubMed 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. Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis.,Lu D, Silhan J, Macdonald JT, Carpenter EP, Jensen K, Tang CM, Baldwin GS, Freemont PS Proc Natl Acad Sci U S A. 2012 Oct 3. PMID:23035246 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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