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Crystallization and preliminary X-ray diffraction analysis of ribosomal protein L11 methyltransferase from Thermus thermophilus HB8.
Kaminishi, Tatsuya; Sakai, Hiroaki; Takemoto-Hori, Chie; Terada, Takaho; Nakagawa, Noriko; Maoka, Nobuko; Kuramitsu, Seiki; Shirouzu, Mikako; Yokoyama, Shigeyuki.
Afiliação
  • Kaminishi T; RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Acta Crystallogr D Biol Crystallogr ; 59(Pt 5): 930-2, 2003 May.
Article em En | MEDLINE | ID: mdl-12777815
ABSTRACT
Ribosomal proteins are subjected to a variety of post-translational modifications, of which methylation is the most frequently found in all three kingdoms of life. PrmA is the only bacterial enzyme identified to date that catalyzes the methylation of a ribosomal protein. It is responsible for the introduction of nine methyl groups into the N-terminal domain of ribosomal protein L11. The PrmA protein from Thermus thermophilus HB8 was crystallized and a preliminary X-ray diffraction analysis was performed. A cryocooled crystal diffracted X-rays beyond 1.9 A using synchrotron radiation.
Assuntos
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Base de dados: MEDLINE Assunto principal: Proteínas Ribossômicas / Thermus thermophilus / Metiltransferases Idioma: En Revista: Acta Crystallogr D Biol Crystallogr Ano de publicação: 2003 Tipo de documento: Article País de afiliação: Japão
Buscar no Google
Base de dados: MEDLINE Assunto principal: Proteínas Ribossômicas / Thermus thermophilus / Metiltransferases Idioma: En Revista: Acta Crystallogr D Biol Crystallogr Ano de publicação: 2003 Tipo de documento: Article País de afiliação: Japão