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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1998-1-6
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pubmed:abstractText |
The three-dimensional solution structure has been determined by NMR spectroscopy of the 75 residue C-terminal domain of ribosomal protein L11 (L11-C76) in its RNA-bound state. L11-C76 recognizes and binds tightly to a highly conserved 58 nucleotide domain of 23 S ribosomal RNA, whose secondary structure consists of three helical stems and a central junction loop. The NMR data reveal that the conserved structural core of the protein, which consists of a bundle of three alpha-helices and a two-stranded parallel beta-sheet four residues in length, is nearly the same as the solution structure determined for the non-liganded form of the protein. There are however, substantial chemical shift perturbations which accompany RNA binding, the largest of which map onto an extended loop which bridges the C-terminal end of alpha-helix 1 and the first strand of parallel beta-sheet. Substantial shift perturbations are also observed in the N-terminal end of alpha-helix 1, the intervening loop that bridges helices 2 and 3, and alpha-helix 3. The four contact regions identified by the shift perturbation data also displayed protein-RNA NOEs, as identified by isotope-filtered three-dimensional NOE spectroscopy. The shift perturbation and NOE data not only implicate helix 3 as playing an important role in RNA binding, but also indicate that regions flanking helix 3 are involved as well. Loop 1 is of particular interest as it was found to be flexible and disordered for L11-C76 free in solution, but not in the RNA-bound form of the protein, where it appears rigid and adopts a specific conformation as a result of its direct contact to RNA.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 23S,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L11
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1997 Academic Press Limited.
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
101-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9398519-Amino Acid Sequence,
pubmed-meshheading:9398519-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9398519-Molecular Sequence Data,
pubmed-meshheading:9398519-Protein Conformation,
pubmed-meshheading:9398519-Protein Structure, Secondary,
pubmed-meshheading:9398519-Protein Structure, Tertiary,
pubmed-meshheading:9398519-RNA,
pubmed-meshheading:9398519-RNA, Ribosomal, 23S,
pubmed-meshheading:9398519-RNA-Binding Proteins,
pubmed-meshheading:9398519-Ribosomal Proteins,
pubmed-meshheading:9398519-Solutions
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pubmed:year |
1997
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pubmed:articleTitle |
The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA.
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pubmed:affiliation |
National Institute of Dental Research, Bethesda, MD 20892-4326, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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