1L1T

MutM (Fpg) Bound to Abasic-Site Containing DNA

Summary for 1L1T

• Entry DOI: 10.2210/pdb1l1t/pdb
• Related: 1L1Z 1L2B 1L2C 1L2D
• Descriptor: 5'-D(*AP*G*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3', 5'-D(*TP*GP*C*GP*TP*CP*CP*AP*(HPD)P*GP*TP*CP*TP*AP*CP*C)-3', MutM, ... (5 entities in total)
• Functional Keywords: dna repair, dna glycosylase, zinc finger, hydrolase-dna complex, hydrolase/dna
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 3
• Total formula weight: 40472.18

Authors

Fromme, J.C.,Verdine, G.L. (deposition date: 2002-02-19, release date: 2002-06-14, Last modification date: 2024-02-14)

Primary citation

Fromme, J.C.,Verdine, G.L.
Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM.
Nat.Struct.Biol., 9:544-552, 2002

PubMed Abstract: MutM is a bacterial 8-oxoguanine glycosylase responsible for initiating base-excision repair of oxidized guanine residues in DNA. Here we report five different crystal structures of MutM-DNA complexes that represent different steps of the repair reaction cascade catalyzed by the protein and also differ in the identity of the base opposite the lesion (the 'estranged' base). These structures reveal that the MutM active site performs the multiple steps of base-excision and 3' and 5' nicking with minimal rearrangement of the DNA backbone.

PubMed: 12055620

Experimental method

X-RAY DIFFRACTION (1.8 Å)