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PDBsum entry 2nmv
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Hydrolase/DNA
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PDB id
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2nmv
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References listed in PDB file
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Key reference
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Title
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Damage detection by the uvrabc pathway: crystal structure of uvrb bound to fluorescein-Adducted DNA.
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Authors
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T.R.Waters,
J.Eryilmaz,
S.Geddes,
T.E.Barrett.
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Ref.
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FEBS Lett, 2006,
580,
6423-6427.
[DOI no: ]
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PubMed id
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Abstract
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UvrB is the damage recognition element of the highly conserved UvrABC pathway
that functions in the removal of bulky DNA adducts. Pivotal to this is the
formation of a damage detection complex that relies on the ability of UvrB to
locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA
have recently been reported, none address the issue of lesion recognition. Here,
we describe the crystal structure of UvrB bound to a pentanucleotide containing
a single fluorescein-adducted thymine that reveals a unique mechanism for damage
detection entirely dependent on the exclusion of lesions larger than an
undamaged nucleotide.
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Figure 1.
Fig. 1. (A) The molecular structure of T-fluorescein. (B)
An overview of the UvrB molecule (represented as a molecular
surface) showing the relative locations of the pentathymine
molecule (cyan), the conserved β-hairpin (light green), domains
1a (yellow), 1b (grey), 2 (green) and 3 (pink). (C) A magnified
view of the pentathymine molecule identifying the position of
the T-fluorescein adducted nucleotide, TF3 (magenta), together
with associated F[o] − F[c] omit map density contoured at
2.5σ. The location of the lesion reveals that the damage is
extruded away from the UvrB molecule. PT5 denotes the 5′
phosphate group of T5 that is the only visible moiety of this
nucleotide. All figures were generated using Pymol (Delano
Scientific, www.pymol.org).
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Figure 2.
Fig. 2. Superposition of the pentathymine (light blue),
trithymine (yellow) and stem–loop (grey) UvrB–DNA complexes.
The fluorescein triple ring systems within the stem loop and
pentathymine structures are shown in orange and magenta
respectively.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2006,
580,
6423-6427)
copyright 2006.
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