1dhp
From Proteopedia
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DIHYDRODIPICOLINATE SYNTHASE
Overview
The crystal structure of dihydrodipicolinate synthase from E. coli was, determined by multiple isomorphous replacement methods. The structure was, refined at a resolution of 2.5 A and the final R-factor is 19.6% for, 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The, crystallographic asymmetric unit contains two monomers related by, approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is, built up by crystallographic symmetry. The tetramer is almost planar with, no contacts between the subunits related by the non-crystallographic dyad., The active sites are accessible from a wide water-filled channel in the, center of the tetramer. The dihydrodipicolinate synthase monomer is, composed of two domains. Each polypeptide chain is folded into an 8-fold, alpha/beta barrel and a C-terminal alpha-helical domain comprising, residues 224 to 292. The fold is similar to that of N-acetylneuraminate, lyase. The active site lysine 161 is located in the alpha/beta barrel and, has access via two entrances from the C-terminal side of the barrel.
About this Structure
1DHP is a Single protein structure of sequence from Escherichia coli with K as ligand. Active as Dihydrodipicolinate synthase, with EC number 4.2.1.52 Structure known Active Site: S1. Full crystallographic information is available from OCA.
Reference
The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:7853400
Page seeded by OCA on Mon Nov 5 13:40:38 2007
