3CPR

The crystal structure of Corynebacterium glutamicum dihydrodipicolinate synthase to 2.2 A resolution

Summary for 3CPR

• Entry DOI: 10.2210/pdb3cpr/pdb
• Descriptor: Dihydrodipicolinate synthetase (2 entities in total)
• Functional Keywords: (beta/alpha)8-barrel fold with a c-terminal alpha-helical segment, amino-acid biosynthesis, cytoplasm, diaminopimelate biosynthesis, lyase, lysine biosynthesis, schiff base
• Biological source: Corynebacterium glutamicum (Brevibacterium flavum)
• Cellular location: Cytoplasm : Q546B6
• Total number of polymer chains: 2
• Total formula weight: 63292.06

Authors

Rydel, T.J.,Sturman, E.J.,Rice, E.A. (deposition date: 2008-04-01, release date: 2008-11-18, Last modification date: 2023-11-29)

Primary citation

Rice, E.A.,Bannon, G.A.,Glenn, K.C.,Jeong, S.S.,Sturman, E.J.,Rydel, T.J.
Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein.
Arch.Biochem.Biophys., 480:111-121, 2008

PubMed Abstract: The lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase enzyme (cDHDPS) was recently successfully introduced into maize plants to enhance the level of lysine in the grain. To better understand lysine insensitivity of the cDHDPS, we expressed, purified, kinetically characterized the protein, and solved its X-ray crystal structure. The cDHDPS enzyme has a fold and overall structure that is highly similar to other DHDPS proteins. A noteworthy feature of the active site is the evidence that the catalytic lysine residue forms a Schiff base adduct with pyruvate. Analyses of the cDHDPS structure in the vicinity of the putative binding site for S-lysine revealed that the allosteric binding site in the Escherichia coli DHDPS protein does not exist in cDHDPS due to three non-conservative amino acids substitutions, and this is likely why cDHDPS is not feedback inhibited by lysine.

PubMed: 18930704
DOI: 10.1016/j.abb.2008.09.018

Experimental method

X-RAY DIFFRACTION (2.2 Å)