1RIS

CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN S6 FROM THERMUS THERMOPHILUS

Summary for 1RIS

• Entry DOI: 10.2210/pdb1ris/pdb
• Descriptor: RIBOSOMAL PROTEIN S6 (2 entities in total)
• Functional Keywords: ribosomal protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 11988.75

Authors

Lindahl, M.,Svensson, L.A.,Liljas, A.,Sedelnikova, S.E.,Eliseikina, I.A.,Fomenkova, N.P.,Nevskaya, N.,Nikonov, S.V.,Garber, M.B.,Muranova, T.A.,Rykonova, A.I.,Amons, R. (deposition date: 1994-05-31, release date: 1994-09-30, Last modification date: 2024-02-14)

Primary citation

Lindahl, M.,Svensson, L.A.,Liljas, A.,Sedelnikova, S.E.,Eliseikina, I.A.,Fomenkova, N.P.,Nevskaya, N.,Nikonov, S.V.,Garber, M.B.,Muranova, T.A.,Rykonova, A.I.,Amons, R.
Crystal structure of the ribosomal protein S6 from Thermus thermophilus.
EMBO J., 13:1249-1254, 1994

PubMed Abstract: 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.

PubMed: 8137808

Experimental method

X-RAY DIFFRACTION (2 Å)