1M3H

Crystal Structure of Hogg1 D268E Mutant with Product Oligonucleotide

Summary for 1M3H

• Entry DOI: 10.2210/pdb1m3h/pdb
• Related: 1EBM 1M3Q
• Descriptor: 5'-D(P*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3', 5'-D(P*GP*CP*GP*TP*CP*CP*AP*(DDX))-3', 5'-D(P*GP*TP*CP*TP*AP*CP*C)-3', ... (6 entities in total)
• Functional Keywords: protein-dna complex, end product, dna repair, dna glycosylase, mutant, enzyme, hydrolase-dna complex, hydrolase/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nucleoplasm. Isoform 1A: Nucleus. Isoform 2A: Mitochondrion: O15527
• Total number of polymer chains: 4
• Total formula weight: 44687.29

Authors

Chung, S.J.,Verdine, G.L. (deposition date: 2002-06-27, release date: 2004-04-20, Last modification date: 2024-02-14)

Primary citation

Chung, S.J.,Verdine, G.L.
Structures of End Products Resulting from Lesion Processing by a DNA Glycosylase/Lyase
Chem.Biol., 11:1643-1649, 2004

PubMed 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.

PubMed: 15610848
DOI: 10.1016/j.chembiol.2004.09.014

Experimental method

X-RAY DIFFRACTION (2.05 Å)