2nq9
From Proteopedia
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| - | [[  | + | ==High resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) Y72A mutant bound to damaged DNA==  | 
| + | <StructureSection load='2nq9' size='340' side='right' caption='[[2nq9]], [[Resolution|resolution]] 1.45Å' scene=''>  | ||
| + | == Structural highlights ==  | ||
| + | <table><tr><td colspan='2'>[[2nq9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NQ9 FirstGlance]. <br>  | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>  | ||
| + | <tr><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nfo ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>  | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_IV_(phage-T(4)-induced) Deoxyribonuclease IV (phage-T(4)-induced)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.2 3.1.21.2] </span></td></tr>  | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nq9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nq9 RCSB], [http://www.ebi.ac.uk/pdbsum/2nq9 PDBsum]</span></td></tr>  | ||
| + | <table>  | ||
| + | == 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/nq/2nq9_consurf.spt"</scriptWhenChecked>  | ||
| + |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].  | ||
| + | <div style="clear:both"></div>  | ||
| + | <div style="background-color:#fffaf0;">  | ||
| + | == Publication Abstract from PubMed ==  | ||
| + | Escherichia coli endonuclease IV is an archetype for an abasic or apurinic-apyrimidinic endonuclease superfamily crucial for DNA base excision repair. Here biochemical, mutational and crystallographic characterizations reveal a three-metal ion mechanism for damage binding and incision. The 1.10-A resolution DNA-free and the 2.45-A resolution DNA-substrate complex structures capture substrate stabilization by Arg37 and reveal a distorted Zn3-ligand arrangement that reverts, after catalysis, to an ideal geometry suitable to hold rather than release cleaved DNA product. The 1.45-A resolution DNA-product complex structure shows how Tyr72 caps the active site, tunes its dielectric environment and promotes catalysis by Glu261-activated hydroxide, bound to two Zn2+ ions throughout catalysis. These structural, mutagenesis and biochemical results suggest general requirements for abasic site removal in contrast to features specific to the distinct endonuclease IV alpha-beta triose phosphate isomerase (TIM) barrel and APE1 four-layer alpha-beta folds of the apurinic-apyrimidinic endonuclease families.  | ||
| - | + | DNA apurinic-apyrimidinic site binding and excision by endonuclease IV.,Garcin ED, Hosfield DJ, Desai SA, Haas BJ, Bjoras M, Cunningham RP, Tainer JA Nat Struct Mol Biol. 2008 May;15(5):515-22. Epub 2008 Apr 13. PMID:18408731<ref>PMID:18408731</ref>  | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | |
| - | + | </div>  | |
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==See Also==  | ==See Also==  | ||
*[[Endonuclease|Endonuclease]]  | *[[Endonuclease|Endonuclease]]  | ||
| - | + | == References ==  | |
| - | ==  | + | <references/>  | 
| - | <  | + | __TOC__  | 
| + | </StructureSection>  | ||
[[Category: Escherichia coli]]  | [[Category: Escherichia coli]]  | ||
[[Category: Garcin-Hosfield, E D.]]  | [[Category: Garcin-Hosfield, E D.]]  | ||
Revision as of 04:46, 29 September 2014
High resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) Y72A mutant bound to damaged DNA
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