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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5448
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pubmed:dateCreated |
2000-1-10
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pubmed:databankReference |
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pubmed:abstractText |
Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.
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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/Peptide Elongation Factor G,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Phe,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ribosome releasing factor
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
17
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2349-52
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:10600747-Amino Acid Sequence,
pubmed-meshheading:10600747-Binding Sites,
pubmed-meshheading:10600747-Crystallography, X-Ray,
pubmed-meshheading:10600747-Models, Molecular,
pubmed-meshheading:10600747-Molecular Mimicry,
pubmed-meshheading:10600747-Molecular Sequence Data,
pubmed-meshheading:10600747-Nucleic Acid Conformation,
pubmed-meshheading:10600747-Peptide Elongation Factor G,
pubmed-meshheading:10600747-Protein Biosynthesis,
pubmed-meshheading:10600747-Protein Conformation,
pubmed-meshheading:10600747-Protein Folding,
pubmed-meshheading:10600747-Protein Structure, Secondary,
pubmed-meshheading:10600747-Protein Structure, Tertiary,
pubmed-meshheading:10600747-Proteins,
pubmed-meshheading:10600747-RNA, Bacterial,
pubmed-meshheading:10600747-RNA, Fungal,
pubmed-meshheading:10600747-RNA, Transfer,
pubmed-meshheading:10600747-RNA, Transfer, Phe,
pubmed-meshheading:10600747-Ribosomal Proteins,
pubmed-meshheading:10600747-Ribosomes,
pubmed-meshheading:10600747-Sequence Alignment,
pubmed-meshheading:10600747-Thermotoga maritima
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pubmed:year |
1999
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pubmed:articleTitle |
Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic.
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pubmed:affiliation |
Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Post Office Box 124, SE-22100 Lund, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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