1R2Z

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

Summary for 1R2Z

• Entry DOI: 10.2210/pdb1r2z/pdb
• Related: 1L1T 1L1Z 1L2B 1L2C 1L2D 1R2Y
• Descriptor: 5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3', 5'-D(*TP*GP*CP*GP*TP*CP*CP*AP*(DHU)P*GP*TP*CP*TP*AP*CP*C)-3', MutM, ... (5 entities in total)
• Functional Keywords: dna repair, dna glycosylase, hydrolase-dna complex, hydrolase/dna
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 3
• Total formula weight: 38090.69

Authors

Fromme, J.C.,Verdine, G.L. (deposition date: 2003-09-30, release date: 2003-10-14, Last modification date: 2023-08-23)

Primary citation

Fromme, J.C.,Verdine, G.L.
DNA Lesion Recognition by the Bacterial Repair Enzyme MutM.
J.Biol.Chem., 278:51543-51548, 2003

PubMed Abstract: 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.

PubMed: 14525999
DOI: 10.1074/jbc.M307768200

Experimental method

X-RAY DIFFRACTION (1.63 Å)