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2xhi

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Revision as of 09:27, 11 August 2016

Separation-of-function mutants unravel the dual reaction mode of human 8-oxoguanine DNA glycosylase

Structural highlights

2xhi is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2nof, 2noe, 2i5w, 1lwv, 1n39, 1fn7, 2nol, 2noh, 1ko9, 2nob, 1m3h, 1hu0, 1ebm, 1n3a, 1m3q, 1lww, 1lwy, 2noi, 2noz, 1n3c
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[OGG1_HUMAN] Defects in OGG1 may be a cause of renal cell carcinoma (RCC) [MIM:144700]. It is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma.

Function

[OGG1_HUMAN] DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.

Publication Abstract from PubMed

7,8-Dihydro-8-oxoguanine (8oxoG) is a major mutagenic base lesion formed when reactive oxygen species react with guanine in DNA. The human 8oxoG DNA glycosylase (hOgg1) recognizes and initiates repair of 8oxoG. hOgg1 is acknowledged as a bifunctional DNA glycosylase catalyzing removal of the damaged base followed by cleavage of the backbone of the intermediate abasic DNA (AP lyase/beta-elimination). When acting on 8oxoG-containing DNA, these two steps in the hOgg1 catalysis are considered coupled, with Lys249 implicated as a key residue. However, several lines of evidence point to a concurrent and independent monofunctional hydrolysis of the N-glycosylic bond being the in vivo relevant reaction mode of hOgg1. Here, we present biochemical and structural evidence for the monofunctional mode of hOgg1 by design of separation-of-function mutants. Asp268 is identified as the catalytic residue, while Lys249 appears critical for the specific recognition and final alignment of 8oxoG during the hydrolysis reaction.

Separation-of-Function Mutants Unravel the Dual-Reaction Mode of Human 8-Oxoguanine DNA Glycosylase.,Dalhus B, Forsbring M, Helle IH, Vik ES, Forstrom RJ, Backe PH, Alseth I, Bjoras M Structure. 2011 Jan 12;19(1):117-27. PMID:21220122^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dalhus B, Forsbring M, Helle IH, Vik ES, Forstrom RJ, Backe PH, Alseth I, Bjoras M. Separation-of-Function Mutants Unravel the Dual-Reaction Mode of Human 8-Oxoguanine DNA Glycosylase. Structure. 2011 Jan 12;19(1):117-27. PMID:21220122 doi:10.1016/j.str.2010.09.023

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xhi"

@@ Line 1: / Line 1: @@
 ==Separation-of-function mutants unravel the dual reaction mode of human 8-oxoguanine DNA glycosylase==
 <StructureSection load='2xhi' size='340' side='right' caption='[[2xhi]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=8OG:8-OXO-2-DEOXY-GUANOSINE-5-MONOPHOSPHATE'>8OG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nof|2nof]], [[2noe|2noe]], [[2i5w|2i5w]], [[1lwv|1lwv]], [[1n39|1n39]], [[1fn7|1fn7]], [[2nol|2nol]], [[2noh|2noh]], [[1ko9|1ko9]], [[2nob|2nob]], [[1m3h|1m3h]], [[1hu0|1hu0]], [[1ebm|1ebm]], [[1n3a|1n3a]], [[1m3q|1m3q]], [[1lww|1lww]], [[1lwy|1lwy]], [[2noi|2noi]], [[2noz|2noz]], [[1n3c|1n3c]]</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=2xhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xhi RCSB], [http://www.ebi.ac.uk/pdbsum/2xhi PDBsum]</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=2xhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhi OCA], [http://pdbe.org/2xhi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xhi RCSB], [http://www.ebi.ac.uk/pdbsum/2xhi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xhi ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2xhi" style="background-color:#fffaf0;"></div>
 ==See Also==

2xhi

From Proteopedia

Revision as of 09:27, 11 August 2016

Separation-of-function mutants unravel the dual reaction mode of human 8-oxoguanine DNA glycosylase

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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