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1RL6

RIBOSOMAL PROTEIN L6

Summary for 1RL6
Entry DOI10.2210/pdb1rl6/pdb
DescriptorPROTEIN (RIBOSOMAL PROTEIN L6) (2 entities in total)
Functional Keywordsrna-binding protein, gentamicin resistance, ribosomal protein, alpha/beta protein, rna binding protein
Biological sourceGeobacillus stearothermophilus
Total number of polymer chains1
Total formula weight19202.12
Authors
Golden, B.L.,Davies, C.,Ramakrishnan, V.,White, S.W. (deposition date: 1999-01-14, release date: 1999-02-02, Last modification date: 2023-12-27)
Primary citationGolden, B.L.,Ramakrishnan, V.,White, S.W.
Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein.
EMBO J., 12:4901-4908, 1993
Cited by
PubMed Abstract: In all cells, protein synthesis is coordinated by the ribosome, a large ribonucleoprotein particle that is composed of > 50 distinct protein molecules and several large RNA molecules. Here we present the crystal structure of ribosomal protein L6 from the thermophilic bacterium Bacillus stearothermophilus solved at 2.6 A resolution. L6 contains two domains with almost identical folds, implying that it was created by an ancient gene duplication event. The surface of the molecule displays several likely sites of interaction with other components of the ribosome. The RNA binding sites appear to be localized in the C-terminal domain whereas the N-terminal domain contains the potential sites for protein-protein interactions. The domain structure is homologous with several other ribosomal proteins and to a large family of eukaryotic RNA binding proteins.
PubMed: 8262035
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

238895

数据于2025-07-16公开中

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