4EOU

Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site

Replaces:  3UBS

Summary for 4EOU

• Entry DOI: 10.2210/pdb4eou/pdb
• Related: 1DHP 1YXC 3DU0
• Descriptor: Dihydrodipicolinate synthase, POTASSIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: alpha/beta barrel, tim barrel, amino-acid biosynthesis, schiff base, lyase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6L2
• Total number of polymer chains: 2
• Total formula weight: 63292.70

Authors

Boughton, B.A.,Dobson, R.C.J.,Hutton, C.A. (deposition date: 2012-04-15, release date: 2012-04-25, Last modification date: 2024-11-06)

Primary citation

Boughton, B.A.,Dobson, R.C.,Hutton, C.A.
The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde: Unambiguous resolution of the stereochemistry of the condensation product.
Proteins, 80:2117-2122, 2012

PubMed Abstract: The crystal structure of Escherichia coli dihydrodipicolinate synthase with pyruvate and substrate analogue succinic acid semialdehyde condensed with the active site lysine-161 was solved to a resolution of 2.3 Å. Comparative analysis to a previously reported structure both resolves the configuration at the aldol addition center, where the final addition product clearly displays the (S)-configuration, and the final conformation of the adduct within the active site. Direct comparison to two other crystal structures found in the Protein Data Bank, 1YXC, and 3DU0, demonstrates significant similarity between the active site residues of these structures.

PubMed: 22552955
DOI: 10.1002/prot.24106

Experimental method

X-RAY DIFFRACTION (2.3 Å)