1lww

From Proteopedia

(Difference between revisions)

Revision as of 10:49, 18 October 2017

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

Structural highlights

1lww 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:	1hu0, 1lwv, 1lwy, 1ebm, 1fn7
Gene:	ogg1 (HUMAN)
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.

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

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.

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^[1]

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

References

↑ Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL. Product-assisted catalysis in base-excision DNA repair. Nat Struct Biol. 2003 Mar;10(3):204-11. PMID:12592398 doi:10.1038/nsb902

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lww"

@@ Line 1: / Line 1: @@
 ==Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-bromoguanine==
 <StructureSection load='1lww' size='340' side='right' caption='[[1lww]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hu0|1hu0]], [[1lwv|1lwv]], [[1lwy|1lwy]], [[1ebm|1ebm]], [[1fn7|1fn7]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ogg1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1lww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lww OCA], [http://pdbe.org/1lww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lww RCSB], [http://www.ebi.ac.uk/pdbsum/1lww 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=1lww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lww OCA], [http://pdbe.org/1lww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lww RCSB], [http://www.ebi.ac.uk/pdbsum/1lww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lww ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 21: / Line 22: @@
     <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].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1lww

From Proteopedia

Revision as of 10:49, 18 October 2017

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

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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