1lww

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[[Image:1lww.gif|left|200px]]
 
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{{Structure
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==Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-bromoguanine==
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|PDB= 1lww |SIZE=350|CAPTION= <scene name='initialview01'>1lww</scene>, resolution 2.1&Aring;
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<StructureSection load='1lww' size='340' side='right'caption='[[1lww]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BRG:8-BROMOGUANINE'>BRG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=PED:PENTANE-3,4-DIOL-5-PHOSPHATE'>PED</scene>
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<table><tr><td colspan='2'>[[1lww]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LWW FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE= ogg1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRG:8-BROMOGUANINE'>BRG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PED:PENTANE-3,4-DIOL-5-PHOSPHATE'>PED</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lww OCA], [https://pdbe.org/1lww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lww RCSB], [https://www.ebi.ac.uk/pdbsum/1lww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lww ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1hu0|1HU0]], [[1lwv|1LWV]], [[1lwy|1LWY]], [[1ebm|1EBM]], [[1fn7|1FN7]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lww OCA], [http://www.ebi.ac.uk/pdbsum/1lww PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lww RCSB]</span>
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== Evolutionary Conservation ==
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}}
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lw/1lww_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1lww ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Most spontaneous damage to bases in DNA is corrected through the action of the base-excision DNA repair pathway. Base excision repair is initiated by DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in DNA and catalyze their excision. How such proteins accomplish the feat of catalyzing no fewer than five sequential reaction steps using a single active site has been unknown. To help answer this, we report the structure of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine DNA glycosylase. This structure and supporting biochemical results reveal that the enzyme sequesters the excised lesion base and exploits it as a cofactor to participate in catalysis. To our knowledge, the present example represents the first documented case of product-assisted catalysis in an enzyme-catalyzed reaction.
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'''Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-bromoguanine'''
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Product-assisted catalysis in base-excision DNA repair.,Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL Nat Struct Biol. 2003 Mar;10(3):204-11. PMID:12592398<ref>PMID:12592398</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1lww" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Most spontaneous damage to bases in DNA is corrected through the action of the base-excision DNA repair pathway. Base excision repair is initiated by DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in DNA and catalyze their excision. How such proteins accomplish the feat of catalyzing no fewer than five sequential reaction steps using a single active site has been unknown. To help answer this, we report the structure of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine DNA glycosylase. This structure and supporting biochemical results reveal that the enzyme sequesters the excised lesion base and exploits it as a cofactor to participate in catalysis. To our knowledge, the present example represents the first documented case of product-assisted catalysis in an enzyme-catalyzed reaction.
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*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1LWW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWW OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Product-assisted catalysis in base-excision DNA repair., Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL, Nat Struct Biol. 2003 Mar;10(3):204-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12592398 12592398]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bruner, S D.]]
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[[Category: Bruner SD]]
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[[Category: Fromme, J C.]]
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[[Category: Fromme JC]]
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[[Category: Karplus, M.]]
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[[Category: Karplus M]]
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[[Category: Verdine, G L.]]
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[[Category: Verdine GL]]
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[[Category: Yang, W.]]
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[[Category: Yang W]]
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[[Category: borohydride]]
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[[Category: covalent trapping]]
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[[Category: dna glycosylase]]
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[[Category: dna repair]]
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[[Category: product-assisted catalysis]]
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[[Category: protein/dna]]
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[[Category: reaction intermediate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:08:29 2008''
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Current revision

Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-bromoguanine

PDB ID 1lww

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