1ris

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[[Image:1ris.png|left|200px]]
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==CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN S6 FROM THERMUS THERMOPHILUS==
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<StructureSection load='1ris' size='340' side='right' caption='[[1ris]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ris]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RIS FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ris FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ris OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ris RCSB], [http://www.ebi.ac.uk/pdbsum/1ris PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1ris_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1ris| PDB=1ris | SCENE= }}
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Crystal structure of the ribosomal protein S6 from Thermus thermophilus.,Lindahl M, Svensson LA, Liljas A, Sedelnikova SE, Eliseikina IA, Fomenkova NP, Nevskaya N, Nikonov SV, Garber MB, Muranova TA, et al. EMBO J. 1994 Mar 15;13(6):1249-54. PMID:8137808<ref>PMID:8137808</ref>
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===CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN S6 FROM THERMUS THERMOPHILUS===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_8137808}}
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==About this Structure==
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[[1ris]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIS OCA].
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==See Also==
==See Also==
*[[Ribosomal protein S6|Ribosomal protein S6]]
*[[Ribosomal protein S6|Ribosomal protein S6]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:008137808</ref><ref group="xtra">PMID:015103642</ref><ref group="xtra">PMID:015952781</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Amons, R.]]
[[Category: Amons, R.]]

Revision as of 21:54, 28 September 2014

CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN S6 FROM THERMUS THERMOPHILUS

1ris, resolution 2.00Å

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