Abstract
A new peptide deformylase (PDF; EC 3.5.1.27) gene from Leptospira interrogans was identified and cloned into expression plasmid pET22b(+) and was highly expressed in Escherichia coli BL21(DE3). With DEAE-Sepharose anion-exchange chromatography followed by Superdex G-75 size-exclusion chromatography, 60 mg of PDF from L. interrogans was purified from 1 l of cell culture. Crystallization screening of the purified enzyme resulted in two crystal forms, from one of which a 3 A resolution X-ray diffraction data set has been collected.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases*
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Amino Acid Sequence
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Aminopeptidases / chemistry*
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Aminopeptidases / genetics
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Aminopeptidases / isolation & purification
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Aminopeptidases / metabolism*
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Cloning, Molecular
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Crystallography, X-Ray
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Leptospira interrogans / enzymology*
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Molecular Sequence Data
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
Substances
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Recombinant Proteins
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Aminopeptidases
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Amidohydrolases
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peptide deformylase