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PDBsum entry 1thf
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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 evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion.
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Authors
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D.Lang,
R.Thoma,
M.Henn-Sax,
R.Sterner,
M.Wilmanns.
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Ref.
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Science, 2000,
289,
1546-1550.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
0%.
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Abstract
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The atomic structures of two proteins in the histidine biosynthesis pathway
consist of beta/alpha barrels with a twofold repeat pattern. It is likely that
these proteins evolved by twofold gene duplication and gene fusion from a common
half-barrel ancestor. These ancestral domains are not visible as independent
domains in the extant proteins but can be inferred from a combination of
sequence and structural analysis. The detection of subdomain structures may be
useful in efforts to search genome sequences for functionally and structurally
related proteins.
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Figure 1.
Fig. 1. Atomic structures of HisA (upper panel) and HisF (lower
panel) from Thermotoga maritima in ribbon presentations (29).
View from the COOH-terminal face of the central  barrel,
left; side view, center; and view from the NH[2]-terminal face
of the barrel, right. HisF contains two phosphate ions bound to
the active site, shown as space-filling models (red). The strands
and  helices
of the central eightfold / barrel are
in orange and yellow, respectively. Loops at the NH[2]- and
COOH-terminal faces of the barrel are in cyan and green,
respectively. Some loops contain additional secondary structural
elements. The NH[2]- and COOH-termini are labeled when visible.
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Figure 3.
Fig. 3. Model for the evolution of the / barrel
scaffold by twofold gene duplication. The first gene duplication
generates two initially identical half-barrels that are then
fused and adapted into an ancestral / barrel. A
second gene duplication step leads to the diversification of the
ancestral / barrel
into two enzymes with distinct catalytic activities.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2000,
289,
1546-1550)
copyright 2000.
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Secondary reference #1
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Title
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A histidine gene cluster of the hyperthermophile thermotoga maritima: sequence analysis and evolutionary significance.
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Authors
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R.Thoma,
M.Schwander,
W.Liebl,
K.Kirschner,
R.Sterner.
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Ref.
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Extremophiles, 1998,
2,
379-389.
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PubMed id
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