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Literature summary for 4.3.3.7 extracted from

  • Kang, B.S.; Kim, Y.G.; Ahn, J.W.; Kim, K.J.
    Crystal structure of dihydrodipicolinate synthase from Hahella chejuensis at 1.5 A resolution (2010), Int. J. Biol. Macromol., 46, 512-516.
    View publication on PubMed

Application

Application Comment Organism
industry considering the industrial application of this protein, such as its use for lysine biosynthesis, stable conformation via tight tetramerization interfaces may make this valuable protein to be more useful Hahella chejuensis

Cloned(Commentary)

Cloned (Comment) Organism
ligated into the expression vector pET30a and transformed into the Escherichia coli strain B834 for overexpression Hahella chejuensis

Crystallization (Commentary)

Crystallization (Comment) Organism
at 239K using the hanging drop-vapor diffusion method, at 1.5 A resolution. The four subunits of the asymmetric unit assemble to form a tetramer with an approximate 222 symmetry. At the active site, three residues Tyr132, Thr43 and Tyr106 are observed to constitute a catalytic triad. Has a unique extensive dimer–dimer interface that is mediated by strong hydrophobic interactions supplemented by two sets of three hydrogen bonds between four polar residues. Belongs to space group P2(1)2(1)2(1) with cell parameters a = 67.03 A, b = 120.52 A, c = 161.1 A Hahella chejuensis

Organism

Organism UniProt Comment Textmining
Hahella chejuensis Q2S9K4
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Purification (Commentary)

Purification (Comment) Organism
by centrifugation and gel filtration Hahella chejuensis

Subunits

Subunits Comment Organism
tetramer crystallography Hahella chejuensis

Synonyms

Synonyms Comment Organism
DHDPS
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Hahella chejuensis
dihydrodipicolinate synthase
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Hahella chejuensis