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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5364
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pubmed:dateCreated |
1998-5-18
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pubmed:databankReference |
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pubmed:abstractText |
The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalytic activity. Mutagenesis and biochemical data indicate that an unusual left-handed betaalphabeta crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor G,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S5
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
752-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9563955-Bacillus subtilis,
pubmed-meshheading:9563955-Binding Sites,
pubmed-meshheading:9563955-Catalysis,
pubmed-meshheading:9563955-Crystallography, X-Ray,
pubmed-meshheading:9563955-Endoribonucleases,
pubmed-meshheading:9563955-Evolution, Molecular,
pubmed-meshheading:9563955-Magnesium,
pubmed-meshheading:9563955-Models, Molecular,
pubmed-meshheading:9563955-Peptide Elongation Factor G,
pubmed-meshheading:9563955-Peptide Elongation Factors,
pubmed-meshheading:9563955-Protein Biosynthesis,
pubmed-meshheading:9563955-Protein Conformation,
pubmed-meshheading:9563955-Protein Folding,
pubmed-meshheading:9563955-Protein Structure, Secondary,
pubmed-meshheading:9563955-RNA, Bacterial,
pubmed-meshheading:9563955-RNA, Catalytic,
pubmed-meshheading:9563955-Ribonuclease P,
pubmed-meshheading:9563955-Ribosomal Proteins,
pubmed-meshheading:9563955-Zinc
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pubmed:year |
1998
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pubmed:articleTitle |
Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
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pubmed:affiliation |
Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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