Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

Hongfei Wang, Chie Hori Takemoto, Kazutaka Murayama, Hiroaki Sakai, Ayako Tatsuguchi, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Ribosomal protein L27 is located near the peptidyltransferase center at the interface of ribosomal subunits, and is important for ribosomal assembly and function. We report the crystal structure of ribosomal protein L27 from Thermus thermophilus HB8, which was determined by the multiwavelength anomalous dispersion method and refined to an R-factor of 19.7% (Rfree = 23.6%) at 2.8 Å resolution. The overall fold is an all β-sheet hybrid. It consists of two sets of four-stranded β-sheets formed around a well-defined hydrophobic core, with a highly positive charge on the protein surface. The structure of ribosomal protein L27 from T. thermophilus HB8 in the RNA-free form is investigated, and its functional roles in the ribosomal subunit are discussed.

Original languageEnglish
Pages (from-to)2806-2810
Number of pages5
JournalProtein Science
Volume13
Issue number10
DOIs
Publication statusPublished - 2004 Oct
Externally publishedYes

Keywords

  • Crystal structure
  • Protein-RNA interactions
  • Ribosomal protein L27
  • Ribosome
  • Thermus thermophilus HB8

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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