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Preparation, Crystallization and Preliminary X-Ray Analysis of Threonine Synthase from Streptococcus mutans

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Abstract:

The thrC gene of Streptococcus mutans encodes threonine synthase, which is a potential target for drug design. To study the structure and function of the enzyme, the thrC gene was amplified from Streptococcus mutans genomic DNA and cloned into the expression vector pET28α. The protein was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method. The crystal diffracted to 2.5 Å and belonged to space group P31 or P32, with unit cell parameters a=b=60.39 Å, c=118.62 Å.





Keywords: Protein Purification; Threonine synthase; X-ray diffraction data; polymerase chain reaction amplification; pyridoxal 5-phosphate

Document Type: Research Article

DOI: https://doi.org/10.2174/092986607781483633

Publication date: 2007-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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