Abstract
Research Article15 March 1994free access Crystal structure of the ribosomal protein S6 from Thermus thermophilus. M. Lindahl M. Lindahl Chemical Center, University of Lund, Sweden. Search for more papers by this author L.A. Svensson L.A. Svensson Chemical Center, University of Lund, Sweden. Search for more papers by this author A. Liljas A. Liljas Chemical Center, University of Lund, Sweden. Search for more papers by this author S.E. Sedelnikova S.E. Sedelnikova Chemical Center, University of Lund, Sweden. Search for more papers by this author I.A. Eliseikina I.A. Eliseikina Chemical Center, University of Lund, Sweden. Search for more papers by this author N.P. Fomenkova N.P. Fomenkova Chemical Center, University of Lund, Sweden. Search for more papers by this author N. Nevskaya N. Nevskaya Chemical Center, University of Lund, Sweden. Search for more papers by this author S.V. Nikonov S.V. Nikonov Chemical Center, University of Lund, Sweden. Search for more papers by this author M.B. Garber M.B. Garber Chemical Center, University of Lund, Sweden. Search for more papers by this author T.A. Muranova T.A. Muranova Chemical Center, University of Lund, Sweden. Search for more papers by this author M. Lindahl M. Lindahl Chemical Center, University of Lund, Sweden. Search for more papers by this author L.A. Svensson L.A. Svensson Chemical Center, University of Lund, Sweden. Search for more papers by this author A. Liljas A. Liljas Chemical Center, University of Lund, Sweden. Search for more papers by this author S.E. Sedelnikova S.E. Sedelnikova Chemical Center, University of Lund, Sweden. Search for more papers by this author I.A. Eliseikina I.A. Eliseikina Chemical Center, University of Lund, Sweden. Search for more papers by this author N.P. Fomenkova N.P. Fomenkova Chemical Center, University of Lund, Sweden. Search for more papers by this author N. Nevskaya N. Nevskaya Chemical Center, University of Lund, Sweden. Search for more papers by this author S.V. Nikonov S.V. Nikonov Chemical Center, University of Lund, Sweden. Search for more papers by this author M.B. Garber M.B. Garber Chemical Center, University of Lund, Sweden. Search for more papers by this author T.A. Muranova T.A. Muranova Chemical Center, University of Lund, Sweden. Search for more papers by this author Author Information M. Lindahl1, L.A. Svensson1, A. Liljas1, S.E. Sedelnikova1, I.A. Eliseikina1, N.P. Fomenkova1, N. Nevskaya1, S.V. Nikonov1, M.B. Garber1 and T.A. Muranova1 1Chemical Center, University of Lund, Sweden. The EMBO Journal (1994)13:1249-1254https://doi.org/10.1002/j.1460-2075.1994.tb06376.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The amino acid sequence and crystal structure of the ribosomal protein S6 from the small ribosomal subunit of Thermus thermophilus have been determined. S6 is a small protein with 101 amino acid residues. The 3D structure, which was determined to 2.0 A resolution, consists of a four-stranded anti-parallel beta-sheet with two alpha-helices packed on one side. Similar folding patterns have been observed for other ribosomal proteins and may suggest an original RNA-interacting motif. Related topologies are also found in several other nucleic acid-interacting proteins and based on the assumption that the structure of the ribosome was established early in the molecular evolution, the possibility that an ancestral RNA-interacting motif in ribosomal proteins is the evolutionary origin for the nucleic acid-interacting domain in large classes of ribonucleic acid binding proteins should be considered. Previous ArticleNext Article Volume 13Issue 61 March 1994In this issue RelatedDetailsLoading ...
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