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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2002-7-29
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pubmed:abstractText |
SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Structural observations and data in the literature suggest that this change happens upon mRNA binding.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10205181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10364558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10469640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10628863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10679470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-10781605,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-11053373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-11081631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-11283358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-11511350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-11866529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-1396569,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-2531290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-6113539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-7491491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-7678431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-8052313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-8377180,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12145214-9757107
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/SelB protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0261-4189
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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 |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4145-53
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12145214-Amino Acid Sequence,
pubmed-meshheading:12145214-Amino Acid Substitution,
pubmed-meshheading:12145214-Bacterial Proteins,
pubmed-meshheading:12145214-Binding Sites,
pubmed-meshheading:12145214-Clostridium,
pubmed-meshheading:12145214-Crystallography, X-Ray,
pubmed-meshheading:12145214-Models, Molecular,
pubmed-meshheading:12145214-Molecular Sequence Data,
pubmed-meshheading:12145214-Mutation, Missense,
pubmed-meshheading:12145214-Peptide Elongation Factors,
pubmed-meshheading:12145214-Protein Conformation,
pubmed-meshheading:12145214-Protein Structure, Tertiary,
pubmed-meshheading:12145214-RNA, Bacterial,
pubmed-meshheading:12145214-RNA, Messenger,
pubmed-meshheading:12145214-RNA, Transfer,
pubmed-meshheading:12145214-Ribosomes,
pubmed-meshheading:12145214-Sequence Alignment,
pubmed-meshheading:12145214-Sequence Homology, Amino Acid,
pubmed-meshheading:12145214-Sulfates
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pubmed:year |
2002
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pubmed:articleTitle |
Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.
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pubmed:affiliation |
Department of Molecular Biophysics, Lund University, PO Box 124, S-221 00 Lund, Sweden. maria@mrc-lmb.cam.ac.uk
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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