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1h6j

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Revision as of 15:29, 2 May 2008 by OCA (Talk | contribs)
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Template:STRUCTURE 1h6j

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 Fri May 2 18:29:46 2008

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