1rl6

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{{STRUCTURE_1rl6| PDB=1rl6 | SCENE= }}
{{STRUCTURE_1rl6| PDB=1rl6 | SCENE= }}
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'''RIBOSOMAL PROTEIN L6'''
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===RIBOSOMAL PROTEIN L6===
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==Overview==
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In all cells, protein synthesis is coordinated by the ribosome, a large ribonucleoprotein particle that is composed of &gt; 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.
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{{ABSTRACT_PUBMED_8262035}}
==About this Structure==
==About this Structure==
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[[Category: Ribosomal protein]]
[[Category: Ribosomal protein]]
[[Category: Rna-binding protein]]
[[Category: Rna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:38:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:53:25 2008''

Revision as of 09:53, 29 July 2008

Image:1rl6.png

Template:STRUCTURE 1rl6

RIBOSOMAL PROTEIN L6

Template:ABSTRACT PUBMED 8262035

About this Structure

1RL6 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein., Golden BL, Ramakrishnan V, White SW, EMBO J. 1993 Dec 15;12(13):4901-8. PMID:8262035

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