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PDBsum entry 1dts
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References listed in PDB file
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Key reference
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Title
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Crystal structure of an ATP-Dependent carboxylase, Dethiobiotin synthetase, At 1.65 a resolution.
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Authors
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W.Huang,
Y.Lindqvist,
G.Schneider,
K.J.Gibson,
D.Flint,
G.Lorimer.
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Ref.
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Structure, 1994,
2,
407-414.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: In Escherichia coli, the enzymes of the biotin biosynthesis pathway
are encoded by the bio operon. One of these enzymes, ATP-dependent dethiobiotin
synthetase, catalyzes the carboxylation of 7,8-diaminopelargonic acid leading to
the formation of the ureido ring of biotin. The enzyme belongs to the class of
ATP-dependent carboxylases and we present here the first crystal structure
determined for this class of enzyme. RESULTS: We have determined the crystal
structure of homodimeric dethiobiotin synthetase to 1.65 A resolution. The
subunit consists of a seven-stranded parallel beta-sheet, surrounded by
alpha-helices. The sheet contains the classical mononucleotide-binding motif
with a fingerprint peptide Gly-X-X-X-X-X-Gly-Lys-Thr. The mononucleotide binding
part of the structure is very similar to the GTP-binding protein H-ras-p21 and
thus all GTP-binding proteins. A comparison reveals that some of the residues,
which in H-ras-p21 interact with the nucleotide and the metal ion, are conserved
in the synthetase. CONCLUSIONS: The three-dimensional structure of dethiobiotin
synthetase has revealed that ATP-dependent carboxylases contain the classical
mononucleotide-binding fold. Considerable similarities to the structure of the
GTP-binding protein H-ras-p21 were found, indicating that both proteins might
have evolved from a common ancestral mononucleotide-binding fold.
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Figure 9.
Figure 9. Schematic view of the dimer of dethiobiotin
synthetase. The color scheme is that used in Figure 4 and Figure
5. Conserved side chains at the subunit–subunit interface are
included in ball- and-stick representation (for details see
text). The picture was generated with the program MOLSCRIPT
[21]. Figure 9. Schematic view of the dimer of dethiobiotin
synthetase. The color scheme is that used in [3]Figure 4 and
[4]Figure 5. Conserved side chains at the subunit–subunit
interface are included in ball- and-stick representation (for
details see text). The picture was generated with the program
MOLSCRIPT [[5]21].
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Figure 11.
Figure 11. Schematic view of the active site of dethiobiotin
synthetase. The color scheme is that used for Figure 4 and
Figure 5. Conserved polar residues in the vicinity of the
suggested binding site of the γ -phosphate of ATP are shown.
The picture was generated with the program MOLSCRIPT [21].
Figure 11. Schematic view of the active site of dethiobiotin
synthetase. The color scheme is that used for [3]Figure 4 and
[4]Figure 5. Conserved polar residues in the vicinity of the
suggested binding site of the γ -phosphate of ATP are shown.
The picture was generated with the program MOLSCRIPT [[5]21].
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1994,
2,
407-414)
copyright 1994.
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