483d: Difference between revisions

Revision as of 13:26, 3 July 2008

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File:483d.png

Template:STRUCTURE 483d

CRYSTAL STRUCTURE OF THE SARCIN/RICIN DOMAIN FROM E. COLI 23 S RRNACRYSTAL STRUCTURE OF THE SARCIN/RICIN DOMAIN FROM E. COLI 23 S RRNA

Template:ABSTRACT PUBMED 10493875

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: the structure at 1.11 A resolution., Correll CC, Wool IG, Munishkin A, J Mol Biol. 1999 Sep 17;292(2):275-87. PMID:10493875

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 {{STRUCTURE_483d|  PDB=483d  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE SARCIN/RICIN DOMAIN FROM E. COLI 23 S RRNA'''
+===CRYSTAL STRUCTURE OF THE SARCIN/RICIN DOMAIN FROM E. COLI 23 S RRNA===
-==Overview==
+<!--
-The sarcin/ricin domain of 23 S - 28 S ribosomal RNA is essential for protein synthesis because it forms a critical part of the binding site for elongation factors. A crystal structure of an RNA of 27 nucleotides that mimics the domain in Escherichia coli 23 S rRNA was determined at 1.11 A resolution. The domain folds into a hairpin distorted by four non-canonical base-pairs and one base triple. The fold is stabilized by cross-strand and intra-stand stacking; no intramolecular stabilizing metal ions are observed. This is the first structure to reveal in great detail the geometry and the hydration of two common motifs that are conserved in this rRNA domain, a GAGA tetraloop and a G-bulged cross-strand A stack. Differences in the region connecting these motifs to the stem in the E. coli and in the rat sarcin/ricin domains may contribute to the species-specific binding of elongation factors. Correlation of nucleotide protection data with the structure indicates that the domain has two surfaces. One surface is accessible, lies primarily in the major groove, and is likely to bind the elongation factors. The second lies primarily in the minor groove, and is likely to be buried in the ribosome. This minor groove surface includes the Watson-Crick faces of the cytosine bases in the unusual A2654.C2666 and U2653.C2667 water-mediated base-pairs.
+The line below this paragraph, {{ABSTRACT_PUBMED_10493875}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10493875 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10493875}}
 ==About this Structure==
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 [[Category: Wool, I G.]]
 [[Category: Sacin/ricin domain rna recognition ribosomes elongation factors crystal structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:19:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:25:59 2008''