1DHP

DIHYDRODIPICOLINATE SYNTHASE

Summary for 1DHP

• Entry DOI: 10.2210/pdb1dhp/pdb
• Descriptor: DIHYDRODIPICOLINATE SYNTHASE, POTASSIUM ION (3 entities in total)
• Functional Keywords: synthase, dihydrodipicolinate
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6L2
• Total number of polymer chains: 2
• Total formula weight: 62688.07

Authors

Mirwaldt, C.,Korndoerfer, I.,Huber, R. (deposition date: 1995-02-09, release date: 1997-02-12, Last modification date: 2024-02-07)

Primary citation

Mirwaldt, C.,Korndorfer, I.,Huber, R.
The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.
J.Mol.Biol., 246:227-239, 1995

PubMed Abstract: 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.

PubMed: 7853400
DOI: 10.1006/jmbi.1994.0078

Experimental method

X-RAY DIFFRACTION (2.3 Å)