Crystal structure of the ribosomal protein S6 from Thermus thermophilus.
AUTOR(ES)
Lindahl, M
RESUMO
The amino acid sequence and crystal structure of the ribosomal protein S6 from the small ribosomal subunit of Thermus thermophilus have been determined. S6 is a small protein with 101 amino acid residues. The 3D structure, which was determined to 2.0 A resolution, consists of a four-stranded anti-parallel beta-sheet with two alpha-helices packed on one side. Similar folding patterns have been observed for other ribosomal proteins and may suggest an original RNA-interacting motif. Related topologies are also found in several other nucleic acid-interacting proteins and based on the assumption that the structure of the ribosome was established early in the molecular evolution, the possibility that an ancestral RNA-interacting motif in ribosomal proteins is the evolutionary origin for the nucleic acid-interacting domain in large classes of ribonucleic acid binding proteins should be considered.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=394938Documentos Relacionados
- Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.
- Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.
- Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
- Horizontal transference of S-layer genes within Thermus thermophilus.
- The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus