1L2B
MutM (Fpg) DNA End-Product Structure
Summary for 1L2B
Entry DOI | 10.2210/pdb1l2b/pdb |
Related | 1L1T 1L1Z 1L2C 1L2D |
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*C*(AD2))-3', 5'-D(P*GP*TP*CP*TP*AP*CP*C)-3', ... (6 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 | 4 |
Total formula weight | 40309.09 |
Authors | Fromme, J.C.,Verdine, G.L. (deposition date: 2002-02-20, release date: 2002-06-14, Last modification date: 2023-08-16) |
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 Cited by 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: 12055620PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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