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Purification, crystallization and diffraction studies of the methyltransferases BT_2972 and BVU_3255 from antibiotic-resistant pathogens of the genus Bacteroides from the human intestine.


ABSTRACT: The methyltransferases BT_2972 and BVU_3255 from two different Bacteroides species that are antibiotic-resistant pathogens from the human intestine were cloned, overexpressed and purified, yielding approximately 120 mg of each protein from 1 l culture. Apo BT_2972 and BVU_3255 and their complexes with S-adenosylmethionine or S-adenosylhomocysteine were crystallized in four different crystal forms using the hanging-drop vapour-diffusion method. These crystals diffracted to resolutions ranging from 2.8 to 2.2 Å. Sequence analysis suggested that the two proteins are homologous small-molecule methyltransferases.

SUBMITTER: Kumar V 

PROVIDER: S-EPMC3212450 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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Purification, crystallization and diffraction studies of the methyltransferases BT_2972 and BVU_3255 from antibiotic-resistant pathogens of the genus Bacteroides from the human intestine.

Kumar Veerendra V   Mallika Nagarajan N   Sivaraman J J  

Acta crystallographica. Section F, Structural biology and crystallization communications 20111027 Pt 11


The methyltransferases BT_2972 and BVU_3255 from two different Bacteroides species that are antibiotic-resistant pathogens from the human intestine were cloned, overexpressed and purified, yielding approximately 120 mg of each protein from 1 l culture. Apo BT_2972 and BVU_3255 and their complexes with S-adenosylmethionine or S-adenosylhomocysteine were crystallized in four different crystal forms using the hanging-drop vapour-diffusion method. These crystals diffracted to resolutions ranging fro  ...[more]

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