Crystallization and preliminary X-ray diffraction analysis of ribosomal protein L11 methyltransferase from Thermus thermophilus HB8.
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.
Kaminishi
Tatsuya
T
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Sakai
Hiroaki
H
Takemoto-Hori
Chie
C
Terada
Takaho
T
Nakagawa
Noriko
N
Maoka
Nobuko
N
Kuramitsu
Seiki
S
Shirouzu
Mikako
M
Yokoyama
Shigeyuki
S
D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D008780:Methyltransferases / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C027624:ribosomal protein L11; C084165:L11 methyltransferase; D008780:Methyltransferases