Abstract
Cephamycins are broad-spectrum beta-lactam antibiotics that show resistance to certain forms of beta-lactamases. They differ from cephalosporins by the presence of a methoxyl group at the C-7alpha position. The gene products of cmcI and cmcJ are believed to control 7alpha-methoxylation of cephalosporins through successive steps of hydroxylation and methylation. Here, the expression, purification, crystallization and initial data-collection statistics of the 236-amino-acid protein product of cmcI from Streptomyces clavuligerus is reported. The crystals belong to space group P2(1), with unit-cell parameters a = 93.6, b = 182.6, c = 103.2 A, beta = 91.05 degrees. Diffraction data were collected to 2.5 A.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Crystallization
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DNA, Bacterial / chemistry
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / metabolism
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Methyltransferases / biosynthesis
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Methyltransferases / chemistry
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Methyltransferases / metabolism*
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Mixed Function Oxygenases / biosynthesis
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Mixed Function Oxygenases / chemistry
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Mixed Function Oxygenases / metabolism*
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Multienzyme Complexes / biosynthesis
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Multienzyme Complexes / chemistry
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Multienzyme Complexes / metabolism*
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Protein Conformation
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Reverse Transcriptase Polymerase Chain Reaction
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Spectrometry, Mass, Electrospray Ionization
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Streptomyces / chemistry
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Streptomyces / enzymology*
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X-Ray Diffraction
Substances
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DNA, Bacterial
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Multienzyme Complexes
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7-alpha-cephem-methoxylase
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Mixed Function Oxygenases
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Methyltransferases