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PDBsum entry 1itz
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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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Structure and properties of an engineered transketolase from maize.
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Authors
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S.Gerhardt,
S.Echt,
M.Busch,
J.Freigang,
G.Auerbach,
G.Bader,
W.F.Martin,
A.Bacher,
R.Huber,
M.Fischer.
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Ref.
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Plant Physiol, 2003,
132,
1941-1949.
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PubMed id
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Abstract
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The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned
from a cDNA library by southern blotting using a heterologous probe from sorghum
(Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of
Escherichia coli and mature TK of maize was expressed at a high level in E. coli
and cleaved with thrombin, affording plastid TK. The protein in complex with
thiamine pyrophoshate was crystallized, and its structure was solved by
molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to
the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into
three domains. The two topologically equivalent active sites are located in the
subunit interface region and resemble those of the yeast enzyme.
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