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PDBsum entry 1l2c
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Hydrolase/DNA
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PDB id
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1l2c
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural insights into lesion recognition and repair by the bacterial 8-Oxoguanine DNA glycosylase mutm.
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Authors
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J.C.Fromme,
G.L.Verdine.
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Ref.
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Nat Struct Biol, 2002,
9,
544-552.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3. Comparison of active sites from three different stages
of catalysis. a, Active site structure of the rAb  C
recognition complex 6. The density corresponding to the C1' atom
and its hydroxyl is weak, presumably owing to several rotamers
about the C2'-C3' bond.
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Figure 4.
Figure 4. Recognition of the estranged base by MutM. a,
Recognition in the rAb C
complex. b, Recognition in the rAb G
complex. c, Recognition in the rAb T
complex. Dashes indicate hydrogen bonds, and red circles denote
a van der Waals interaction. d−f, Structural formulae
schematics of the mode of recognition seen in (a−c),
respectively.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2002,
9,
544-552)
copyright 2002.
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