1H6J

The three-dimensional structure of capsule-specific CMP:2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli

Summary for 1H6J

• Entry DOI: 10.2210/pdb1h6j/pdb
• Descriptor: 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE (1 entity in total)
• Functional Keywords: nucleotidyltransferase, cmp-kdo synthetase, capsular polysaccharide, saccharide activation
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm (Potential): P42216
• Total number of polymer chains: 2
• Total formula weight: 54119.82

Authors

Jelakovic, S.,Jann, K.,Schulz, G.E. (deposition date: 2001-06-17, release date: 2001-07-12, Last modification date: 2024-05-08)

Primary citation

Jelakovic, S.,Jann, K.,Schulz, G.E.
The Three-Dimensional Structure of Capsule-Specific Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase from Escherichia Coli
FEBS Lett., 391:157-, 1996

PubMed Abstract: 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.

PubMed: 8706906
DOI: 10.1016/0014-5793(96)00724-7

Experimental method

X-RAY DIFFRACTION (2.32 Å)