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

Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):930-2. doi: 10.1107/s0907444903004554. Epub 2003 Apr 25.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Crystallization
  • Methyltransferases / chemistry*
  • Methyltransferases / metabolism
  • Ribosomal Proteins / metabolism*
  • Thermus thermophilus / enzymology*
  • Thermus thermophilus / genetics
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Ribosomal Proteins
  • ribosomal protein L11
  • L11 methyltransferase
  • Methyltransferases