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3c58

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3c58, resolution 1.90Å ()
Ligands: ,
Non-Standard Residues:
Gene: MUTM, FPG (Lactococcus lactis)
Activity: DNA-(apurinic or apyrimidinic site) lyase, with EC number 4.2.99.18
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Crystal structure of a complex between the wild-type lactococcus lactis Fpg (MutM) and a N7-Benzyl-Fapy-dG containing DNA

Publication Abstract from PubMed

Fpg is a bacterial base excision repair enzyme that removes oxidized purines from DNA. This work shows that Fpg and its eukaryote homolog Ogg1 recognize with high affinity FapydG and bulky N7-benzyl-FapydG (Bz-FapydG). The comparative crystal structure analysis of stable complexes between Fpg and carbocyclic cFapydG or Bz-cFapydG nucleoside-containing DNA provides the molecular basis of the ability of Fpg to bind both lesions with the same affinity and to differently process them. To accommodate the steric hindrance of the benzyl group, Fpg selects the adequate rotamer of the extrahelical Bz-cFapydG formamido group, forcing the bulky group to go outside the binding pocket. Contrary to the binding mode of cFapydG, the particular recognition of Bz-cFapydG leads the BER enzymes to unproductive complexes which would hide the lesion and slow down its repair by the NER machinery.

Bacterial base excision repair enzyme Fpg recognizes bulky N7-substituted-FapydG lesion via unproductive binding mode., Coste F, Ober M, Le Bihan YV, Izquierdo MA, Hervouet N, Mueller H, Carell T, Castaing B, Chem Biol. 2008 Jul 21;15(7):706-17. PMID:18635007

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3c58 is a 3 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

See Also

Reference

  • Coste F, Ober M, Le Bihan YV, Izquierdo MA, Hervouet N, Mueller H, Carell T, Castaing B. Bacterial base excision repair enzyme Fpg recognizes bulky N7-substituted-FapydG lesion via unproductive binding mode. Chem Biol. 2008 Jul 21;15(7):706-17. PMID:18635007 doi:S1074-5521(08)00206-8

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