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PDBsum entry 2ido
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References listed in PDB file
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Key reference
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Title
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Structure of the escherichia coli DNA polymerase III epsilon-Hot proofreading complex.
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Authors
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T.W.Kirby,
S.Harvey,
E.F.Derose,
S.Chalov,
A.K.Chikova,
F.W.Perrino,
R.M.Schaaper,
R.E.London,
L.C.Pedersen.
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Ref.
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J Biol Chem, 2006,
281,
38466-38471.
[DOI no: ]
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PubMed id
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Abstract
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The epsilon subunit of Escherichia coli DNA polymerase III possesses
3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon is
tightly bound between the alpha subunit (DNA polymerase) and subunit. Here, we
present the crystal structure of epsilon in complex with HOT, the bacteriophage
P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT interface is
defined by two areas of contact: an interaction of the previously unstructured N
terminus of HOT with an edge of the epsilon central beta-sheet as well as
interactions between HOT and the catalytically important helix alpha1-loop-helix
alpha2 motif of epsilon. This structure provides insight into how HOT and, by
implication, may stabilize the epsilon subunit, thus promoting efficient
proofreading during chromosomal replication.
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Figure 2.
FIGURE 2. Variation in  186 crystallographic
structures. A, superposition of the crystal structures of the
two molecules of 186 in the asymmetric
unit of the 186-HOT complex,
molecule A (blue) and molecule C (red). B, superposition of the
previously determined 186 (green) (Protein
Data Bank code 1J54) with 186 molecule C (red) of
the 186-HOT complex.
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Figure 6.
FIGURE 6. Stereo view of mutator residues. Amino acids of
that
lead to a mutator phenotype when specifically substituted are
shown in red on the structure of the 186-HOT complex. HOT is
in orange, and 186 is in blue. Known
mutator residues are Asp^12 (a), Glu^14 (b), Thr^15 (c), Thr^16
(d), Gly^17 (e), Arg^56 (f), His^66 (g), Val^96 (h), Asp^103
(i), His^162 (j), Ala^161 (k), Asp^167 (m), Leu^171 (n), and
Gly^180 (o).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
38466-38471)
copyright 2006.
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