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Title
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The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli.
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Authors
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S.Jelakovic,
K.Jann,
G.E.Schulz.
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Ref.
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FEBS Lett, 1996,
391,
157-161.
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PubMed id
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Abstract
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CMP-Kdo synthetases from Gram-negative bacteria activate Kdo for incorporation
into lipo- and capsule-polysaccharides. Here we report the crystal structure of
the capsule-specific synthetase from E. coli at 2.3 A resolution. The enzyme is
a dimer of 2 x 245 amino acid residues assuming C2 symmetry. It contains a
central predominantly parallel beta-sheet with surrounding helices. The chain
fold is novel; it is remotely related to a double Rossmann fold. A large pocket
at the carboxyl terminal ends of the central. beta-strands most likely
accommodates the catalytic center. A putative phosphate binding site at the loop
between the first beta-strand and the following helix is indicated by a bound
iridium hexachloride anion.
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