1M3Q: Crystal Structure Of Hogg1 D268e Mutant With Base-Excised Dna And 8-Aminoguanine

Citation:
Abstract
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.
PDB ID: 1M3QDownload
MMDB ID: 103147
PDB Deposition Date: 2002/6/28
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1M3Q: trimeric; determined by author
Molecular Components in 1M3Q
Label Count Molecule
Protein (1 molecule)
1
8-oxoguanine DNA Glycosylase(Gene symbol: OGG1)
Molecule annotation
Nucleotides(2 molecules)
1
5'- D(*gp*gp*tp*ap*gp*ap*cp*cp*tp*gp*gp*ap*cp*gp*c)-3'
Molecule annotation
1
5'-d(*gp*cp*gp*tp*cp*cp*ap*(drz) P*gp*tp*cp*tp*ap*cp*c)-3'
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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