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1L2B

MutM (Fpg) DNA End-Product Structure

Summary for 1L2B
Entry DOI10.2210/pdb1l2b/pdb
Related1L1T 1L1Z 1L2C 1L2D
Descriptor5'-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 Keywordsdna repair, dna glycosylase, zinc finger, hydrolase-dna complex, hydrolase/dna
Biological sourceGeobacillus stearothermophilus
Total number of polymer chains4
Total formula weight40309.09
Authors
Fromme, J.C.,Verdine, G.L. (deposition date: 2002-02-20, release date: 2002-06-14, Last modification date: 2023-08-16)
Primary citationFromme, 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: 12055620
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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