1kfv
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(New page: 200px<br /><applet load="1kfv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kfv, resolution 2.55Å" /> '''Crystal Structure of...)
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Revision as of 17:03, 20 November 2007
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Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.
Overview
The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base, excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide, range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened, purines, from oxidatively damaged DNA. The structure of a non-covalent, complex between the Lactoccocus lactis Fpg and a 1,3-propanediol (Pr), abasic site analogue-containing DNA has been solved. Through an asymmetric, interaction along the damaged strand and the intercalation of the triad, (M75/R109/F111), Fpg pushes out the Pr site from the DNA double helix, recognizing the cytosine opposite the lesion and inducing a 60 degrees, bend of the DNA. The specific recognition of this cytosine provides some, structural basis for understanding the divergence between Fpg and its, structural homologue endo nuclease VIII towards their substrate, specificities. In addition, the modelling of the 8-oxoguanine residue, allows us to define an enzyme pocket that may accommodate the extrahelical, oxidized base.
About this Structure
1KFV is a Single protein structure of sequence from Lactococcus lactis with ZN and GOL as ligands. Active as DNA-formamidopyrimidine glycosylase, with EC number 3.2.2.23 Full crystallographic information is available from OCA.
Reference
Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA., Serre L, Pereira de Jesus K, Boiteux S, Zelwer C, Castaing B, EMBO J. 2002 Jun 17;21(12):2854-65. PMID:12065399
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