1ko9
From Proteopedia
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|PDB= 1ko9 |SIZE=350|CAPTION= <scene name='initialview01'>1ko9</scene>, resolution 2.15Å | |PDB= 1ko9 |SIZE=350|CAPTION= <scene name='initialview01'>1ko9</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= OGG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= OGG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ebm|1EBM]], [[1fn7|1FN7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ko9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ko9 OCA], [http://www.ebi.ac.uk/pdbsum/1ko9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ko9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Seeberg, E.]] | [[Category: Seeberg, E.]] | ||
| - | [[Category: SO4]] | ||
[[Category: helix-hairpin-helix dna-glycosylase]] | [[Category: helix-hairpin-helix dna-glycosylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:16 2008'' |
Revision as of 18:51, 30 March 2008
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| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | OGG1 (Homo sapiens) | ||||||
| Related: | 1EBM, 1FN7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Native Structure of the Human 8-oxoguanine DNA Glycosylase hOGG1
Contents |
Overview
Both 8oxo-guanine and formamidopyrimidines are major products of oxidative DNA damage that can result in the fixation of transversion mutations following replication if left unrepaired. These lesions are targeted by the N-DNA glycosylase hOgg1, which catalyses excision of the aberrant base followed by cleavage of the phosphate backbone directly 5' to the resultant abasic site in a context, dependent manner. We present the crystal structure of native hOgg1 refined to 2.15 A resolution that reveals a number of highly significant conformational changes on association with DNA that are clearly required for substrate recognition and specificity. Changes of this magnitude appear to be unique to hOgg1 and have not been observed in any of the DNA-glycosylase structures analysed to date where both native and DNA-bound forms are available. It has been possible to identify a mechanism whereby the catalytic residue Lys 249 is "primed" for nucleophilic attack of the N-glycosidic bond.
Disease
Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]
About this Structure
1KO9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase., Bjoras M, Seeberg E, Luna L, Pearl LH, Barrett TE, J Mol Biol. 2002 Mar 22;317(2):171-7. PMID:11902834
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