1ris

<StructureSection load='1ris' size='340' side='right' caption='[[1ris]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<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>

</td></tr><tr id='resources'><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>

[[http://www.uniprot.org/uniprot/RS6_THETH RS6_THETH]] Located on the outer edge of the platform on the body of the 30S subunit (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1ris_consurf.spt"</scriptWhenChecked>

</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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

<references/>

[[Category: Amons, R]]

[[Category: Eliseikina, I A]]

[[Category: Fomenkova, N P]]

[[Category: Garber, M B]]

[[Category: Liljas, A]]

[[Category: Lindahl, M]]

[[Category: Muranova, T A]]

[[Category: Nevskaya, N]]

[[Category: Nikonov, S V]]

[[Category: Rykonova, A I]]

[[Category: Sedelnikova, S E]]

[[Category: Svensson, L A]]

[[Category: Ribosomal protein]]