Crystallization and preliminary X-ray diffraction analysis of ribosomal protein L11 methyltransferase from Thermus thermophilus HB8.
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.
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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