4b5f
From Proteopedia
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| - | [[ | + | ==Substrate bound Neisseria AP endonuclease in absence of metal ions (crystal form 1)== |
| + | <StructureSection load='4b5f' size='340' side='right' caption='[[4b5f]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4b5f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B5F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B5F FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b5g|4b5g]], [[4b5h|4b5h]], [[4b5i|4b5i]], [[4b5j|4b5j]], [[4b5m|4b5m]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b5f RCSB], [http://www.ebi.ac.uk/pdbsum/4b5f PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:23035246</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Exodeoxyribonuclease III]] | [[Category: Exodeoxyribonuclease III]] | ||
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
| - | [[Category: Baldwin, G S | + | [[Category: Baldwin, G S]] |
| - | [[Category: Carpenter, E P | + | [[Category: Carpenter, E P]] |
| - | [[Category: Freemont, P S | + | [[Category: Freemont, P S]] |
| - | [[Category: Jensen, K | + | [[Category: Jensen, K]] |
| - | [[Category: Lu, D | + | [[Category: Lu, D]] |
| - | [[Category: Macdonald, J T | + | [[Category: Macdonald, J T]] |
| - | [[Category: Silhan, J | + | [[Category: Silhan, J]] |
| - | [[Category: Tang, C M | + | [[Category: Tang, C M]] |
[[Category: Hydrolase-dna complex]] | [[Category: Hydrolase-dna complex]] | ||
Revision as of 15:03, 9 December 2014
Substrate bound Neisseria AP endonuclease in absence of metal ions (crystal form 1)
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