1m3h

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File:1m3h.gif


1m3h, resolution 2.05Å

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Crystal Structure of Hogg1 D268E Mutant with Product Oligonucleotide

OverviewOverview

DNA glycosylase/lyases initiate the repair of damaged nucleobases in the genome by catalyzing excision of aberrant nucleobases and nicking of the lesion-containing DNA strand. Nearly all of these proteins have the unusual property of remaining tightly bound in vitro to the end products of the reaction cascade. We have taken advantage of this property to crystallize and structurally characterize the end product resulting from complete DNA processing by a catalytically active mutant form of human 8-oxoguanine DNA glycosylase (D268E hOgg1). The resulting structure is consistent with the currently accepted catalytic mechanism for the protein. Unexpectedly, however, soaking of a nucleobase analog into the crystals results in religation of the DNA backbone in situ.

DiseaseDisease

Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]

About this StructureAbout this Structure

1M3H is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structures of end products resulting from lesion processing by a DNA glycosylase/lyase., Chung SJ, Verdine GL, Chem Biol. 2004 Dec;11(12):1643-9. PMID:15610848

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