Literature DB >> 15340170

Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8.

Hongfei Wang1, Chie Hori Takemoto, Kazutaka Murayama, Hiroaki Sakai, Ayako Tatsuguchi, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama.   

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% (R(free) = 23.6%) at 2.8 A resolution. The overall fold is an all beta-sheet hybrid. It consists of two sets of four-stranded beta-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.

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Year:  2004        PMID: 15340170      PMCID: PMC2286543          DOI: 10.1110/ps.04864904

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  24 in total

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