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Literature summary for 2.3.1.179 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene fabF, subcloning in Escherichia coli strain XL1-Blue, expression in Escherichia coli strain BL21(DE3) Streptococcus pneumoniae

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Streptococcus pneumoniae Q9FBC2 gene fabF
-

Synonyms

Synonyms Comment Organism
FabF
-
Streptococcus pneumoniae