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| | <StructureSection load='3fhg' size='340' side='right'caption='[[3fhg]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3fhg' size='340' side='right'caption='[[3fhg]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fhg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fhg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fhf|3fhf]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">1451601, MJ0724, ogg, SSO0904 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhg OCA], [https://pdbe.org/3fhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhg RCSB], [https://www.ebi.ac.uk/pdbsum/3fhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhg ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhg OCA], [https://pdbe.org/3fhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhg RCSB], [https://www.ebi.ac.uk/pdbsum/3fhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/OGG1_SULSO OGG1_SULSO]] Responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 7-oxoG) from DNA. Also nicks DNA at apurinic/apyrimidinic sites (AP sites).[HAMAP-Rule:MF_00241]
| + | [https://www.uniprot.org/uniprot/OGG1_SACS2 OGG1_SACS2] Catalyzes the excision of an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA. Also cleaves the DNA backbone at apurinic/apyrimidinic sites (AP sites).[HAMAP-Rule:MF_00241] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Doublie, S]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Faucher, F]] | + | [[Category: Doublie S]] |
| - | [[Category: 8-oxog]] | + | [[Category: Faucher F]] |
| - | [[Category: 8-oxoguanine]]
| + | |
| - | [[Category: Dna damage]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Glycosylase]]
| + | |
| - | [[Category: Helix-hairpin-helix]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Multifunctional enzyme]]
| + | |
| - | [[Category: Nuclease]]
| + | |
| - | [[Category: Ogg]]
| + | |
| - | [[Category: Ssogg]]
| + | |
| Structural highlights
Function
OGG1_SACS2 Catalyzes the excision of an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA. Also cleaves the DNA backbone at apurinic/apyrimidinic sites (AP sites).[HAMAP-Rule:MF_00241]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Among the four DNA bases, guanine is particularly vulnerable to oxidative damage and the most common oxidative product, 7,8-dihydro-8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. Fortunately, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Ogg enzymes are divided into three separate families, namely, Ogg1, Ogg2, and archaeal GO glycosylase (AGOG). To date, structures of members of both Ogg1 and AGOG families are known but no structural information is available for members of Ogg2. Here we describe the first crystal structures of two archaeal Ogg2: Methanocaldococcus janischii Ogg and Sulfolobus solfataricus Ogg. A structural comparison with OGG1 and AGOG suggested that the C-terminal lysine of Ogg2 may play a key role in discriminating between guanine and 8-oxoG. This prediction was substantiated by measuring the glycosylase/lyase activity of a C-terminal deletion mutant of MjaOgg.
Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction.,Faucher F, Duclos S, Bandaru V, Wallace SS, Doublie S Structure. 2009 May 13;17(5):703-12. PMID:19446526[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Faucher F, Duclos S, Bandaru V, Wallace SS, Doublie S. Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction. Structure. 2009 May 13;17(5):703-12. PMID:19446526 doi:10.1016/j.str.2009.03.007
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