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1r2z

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1r2z, resolution 1.63Å ()
Ligands:
Non-Standard Residues:
Gene: mutm (Geobacillus stearothermophilus)
Related: 1l1t, 1l1z, 1l2b, 1l2c, 1l2d, 1r2y
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

MutM (Fpg) bound to 5,6-dihydrouracil (DHU) containing DNA

Publication Abstract from PubMed

MutM is a bacterial DNA glycosylase that removes the mutagenic lesion 8-oxoguanine (oxoG) from duplex DNA. The means of oxoG recognition by MutM (also known as Fpg) is of fundamental interest, in light of the vast excess of normal guanine bases present in genomic DNA. The crystal structure of a recognition-competent but catalytically inactive version of MutM in complex with oxoG-containing DNA reveals the structural basis for recognition. MutM binds the oxoG nucleoside in the syn glycosidic configuration and distinguishes oxoG from guanine by reading out the protonation state of the N7 atom. The segment of MutM principally responsible for oxoG recognition is a flexible loop, suggesting that conformational mobility influences lesion recognition and catalysis. Furthermore, the structure of MutM in complex with DNA containing an alternative substrate, dihydrouracil, demonstrates how MutM is able to recognize lesions other than oxoG.

DNA lesion recognition by the bacterial repair enzyme MutM., Fromme JC, Verdine GL, J Biol Chem. 2003 Dec 19;278(51):51543-8. Epub 2003 Oct 1. PMID:14525999

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

About this Structure

1r2z is a 3 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

See Also

Reference

  • Fromme JC, Verdine GL. DNA lesion recognition by the bacterial repair enzyme MutM. J Biol Chem. 2003 Dec 19;278(51):51543-8. Epub 2003 Oct 1. PMID:14525999 doi:10.1074/jbc.M307768200

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