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 (Comment) | Organism |
---|---|
ligated into the expression vector pET30a and transformed into the Escherichia coli strain B834 for overexpression | Hahella chejuensis |
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 dimerdimer 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 | UniProt | Comment | Textmining |
---|---|---|---|
Hahella chejuensis | Q2S9K4 | - |
- |
Purification (Comment) | Organism |
---|---|
by centrifugation and gel filtration | Hahella chejuensis |
Subunits | Comment | Organism |
---|---|---|
tetramer | crystallography | Hahella chejuensis |
Synonyms | Comment | Organism |
---|---|---|
DHDPS | - |
Hahella chejuensis |
dihydrodipicolinate synthase | - |
Hahella chejuensis |