1RIS: CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN S6 FROM THERMUS THERMOPHILUS

Citation:
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.
PDB ID: 1RISDownload
MMDB ID: 51176
PDB Deposition Date: 1994/5/31
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1RIS: tetrameric; determined by author
Molecular Components in 1RIS
Label Count Molecule
Proteins (4 molecules)
4
Ribosomal Protein S6
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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