Literature summary extracted from
Parthasarathy, G.; Cummings, R.; Becker, J.W.; Soisson, S.M.
Surface-entropy reduction approaches to manipulate crystal forms of beta-ketoacyl acyl carrier protein synthase II from Streptococcus pneumoniae (2008), Acta Crystallogr. Sect. D, 64, 141-148.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.3.1.179 |
gene fabF, subcloning in Escherichia coli strain XL1-Blue, expression in Escherichia coli strain BL21(DE3) |
Streptococcus pneumoniae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.3.1.179 |
purified recombinant wild-type and mutant E383A enzymes, hanging-drop vapour-diffusion method at room temperature, 0.001 ml of protein solution, containing 10 mg/mlprotein in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, and 10% glycerol, is mixed with 0.001 ml of precipitating solution, containing 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, and 30% PEG 4000, formation of different crystal forms, X-ray diffraction structure determinations and analysis at 1.3-2.1 A resolution |
Streptococcus pneumoniae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.3.1.179 |
E383A |
crystal structure determination and comparison to the wild-type enzyme, the mutation E383A appears to play a key role in disfavouring the less desirable triclinic crystal form and in generating a new surface for a packing interaction that stabilizes the new crystal form |
Streptococcus pneumoniae |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.3.1.179 |
Streptococcus pneumoniae |
Q9FBC2 |
gene fabF |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.3.1.179 |
FabF |
- |
Streptococcus pneumoniae |