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The three‐dimensional structure of capsule‐specific CMP: 2‐keto‐3‐deoxy‐ manno ‐octonic acid synthetase from Escherichia coli
Author(s) -
Jelakovic Stefan,
Jann Klaus,
Schulz Georg E.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00724-7
Subject(s) - dimer , escherichia coli , stereochemistry , chemistry , enzyme , transferase , amino acid , active site , capsule , binding site , biochemistry , nucleotide , biology , organic chemistry , botany , gene
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 Å resolution. The enzyme is a dimer of 2 × 245 amino acid residues assuming C 2 symmetry. It contains a central predominantly parallel β‐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 β‐strands most likely accommodates the catalytic center. A putative phosphate binding site at the loop between the first β‐strand and the following helix is indicated by a bound iridium hexachloride anion.