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 |
Published |
United States
01.09.2004
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Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0907-4449 |