Expression, purification, crystallization and preliminary X-ray diffraction studies of the cmcI component of Streptomyces clavuligerus 7alpha-cephem-methoxylase
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 cephalospo...
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Published in | Acta crystallographica. Section D, Biological crystallography. Vol. 60; no. Pt 9; pp. 1618 - 1621 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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United States
01.09.2004
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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. |
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AbstractList | 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. |
Author | Svenda, Martin Oster, Linda M Andersson, Inger Lester, Diane R |
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Snippet | Cephamycins are broad-spectrum beta-lactam antibiotics that show resistance to certain forms of beta-lactamases. They differ from cephalosporins by the... |
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SubjectTerms | Crystallization DNA, Bacterial - chemistry Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism Methyltransferases - biosynthesis Methyltransferases - chemistry Methyltransferases - metabolism Mixed Function Oxygenases - biosynthesis Mixed Function Oxygenases - chemistry Mixed Function Oxygenases - metabolism Multienzyme Complexes - biosynthesis Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism Protein Conformation Reverse Transcriptase Polymerase Chain Reaction Spectrometry, Mass, Electrospray Ionization Streptomyces - chemistry Streptomyces - enzymology X-Ray Diffraction |
Title | Expression, purification, crystallization and preliminary X-ray diffraction studies of the cmcI component of Streptomyces clavuligerus 7alpha-cephem-methoxylase |
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