1h6j
From Proteopedia
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| , resolution 2.32Å | |||||||
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| Activity: | 3-deoxy-manno-octulosonate cytidylyltransferase, with EC number 2.7.7.38 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1H6J is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli., Jelakovic S, Jann K, Schulz GE, FEBS Lett. 1996 Aug 5;391(1-2):157-61. PMID:8706906
Page seeded by OCA on Thu Mar 20 11:32:57 2008
