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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2003-11-20
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pubmed:databankReference |
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pubmed:abstractText |
The ribosomal protein S28E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. Sequence homologs of S28E are found only in archaea and eukaryotes. Here we report the three-dimensional solution structure of S28E by NMR spectroscopy. S28E contains a globular region and a long C-terminal tail protruding from the core. The globular region consists of four antiparallel beta-strands that are arranged in a Greek-key topology. Unique features of S28E include an extended loop L2-3 that folds back onto the protein and a 12-residue charged C-terminal tail with no regular secondary structure and greater flexibility relative to the rest of the protein. The structural and surface resemblance to OB-fold family of proteins and the presence of highly conserved basic residues suggest that S28E may bind to RNA. A broad positively charged surface extending over one side of the beta-barrel and into the flexible C terminus may present a putative binding site for RNA.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-10212987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-10562565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-10778738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-10937989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11080142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11080635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11352591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11752303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11854485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11866529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-11909526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-12051947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-12490706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-12557191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-7830604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-8377180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-8458342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-8520220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-8608120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-8743704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-8990123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-9008363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-9192068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14627743-9757107
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0961-8368
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pubmed:author |
pubmed-author:ArrowsmithCheryl HCH,
pubmed-author:CortJohn RJR,
pubmed-author:DyeII,
pubmed-author:EdwardsAledA,
pubmed-author:JungJin-WonJW,
pubmed-author:KennedyMichaelM,
pubmed-author:LeeWeontaeW,
pubmed-author:Pineda-LucenaAntonioA,
pubmed-author:RamelotTheresa ATA,
pubmed-author:SemesiAnthonyA,
pubmed-author:YeeAdelindaA
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2831-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14627743-Amino Acid Sequence,
pubmed-meshheading:14627743-Bacterial Proteins,
pubmed-meshheading:14627743-Methanobacterium,
pubmed-meshheading:14627743-Models, Molecular,
pubmed-meshheading:14627743-Molecular Sequence Data,
pubmed-meshheading:14627743-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:14627743-Protein Conformation,
pubmed-meshheading:14627743-Protein Folding,
pubmed-meshheading:14627743-Ribosomal Proteins,
pubmed-meshheading:14627743-Sequence Alignment,
pubmed-meshheading:14627743-Structure-Activity Relationship
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pubmed:year |
2003
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pubmed:articleTitle |
Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum.
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pubmed:affiliation |
Northeast Structural Genomics Consortium, Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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