2kjw: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[2kjw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KJW FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kjw OCA], [https://pdbe.org/2kjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kjw RCSB], [https://www.ebi.ac.uk/pdbsum/2kjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kjw ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kjw OCA], [https://pdbe.org/2kjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kjw RCSB], [https://www.ebi.ac.uk/pdbsum/2kjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kjw ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/RS6_THET8 RS6_THET8] Located on the outer edge of the platform on the body of the 30S subunit.[HAMAP-Rule:MF_00360]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The ribosomal protein S6 from Thermus thermophilus has served as a model system for the study of protein folding, especially for understanding the effects of circular permutations of secondary structure elements. This study presents the structure of a permutant protein, the 96-residue P(54-55), and the structure of its 101-residue parent protein S6(wt) in solution. The data also characterizes the effects of circular permutation on the backbone dynamics of S6. Consistent with crystallographic data on S6(wt), the overall solution structures of both P(54-55) and S6(wt) show a beta-sheet of four antiparallel beta-strands with two alpha-helices packed on one side of the sheet. In clear contrast to the crystal data, however, the solution structure of S6(wt) reveals a disordered loop in the region between beta-strands 2 and 3 (Leu43-Phe60) instead of a well-ordered stretch and associated hydrophobic mini-core observed in the crystal structure. Moreover, the data for P(54-55) show that the joined wild-type N- and C-terminals form a dynamically robust stretch with a hairpin structure that complies with the in silico design. Taken together, the results explain why the loop region of the S6(wt) structure is relatively insensitive to mutational perturbations, and why P(54-55) is more stable than S6(wt): the permutant incision at Lys54-Asp55 is energetically neutral by being located in an already disordered loop whereas the new hairpin between the wild-type N- and C-termini is stabilizing.
-Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).,Ohman A, Oman T, Oliveberg M Protein Sci. 2010 Jan;19(1):183-9. PMID:19937661<ref>PMID:19937661</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2kjw" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ribosomal protein S6|Ribosomal protein S6]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>