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| | <StructureSection load='2bxj' size='340' side='right'caption='[[2bxj]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2bxj' size='340' side='right'caption='[[2bxj]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bxj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BXJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bxj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BXJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cqm|1cqm]], [[1cqn|1cqn]], [[1eg0|1eg0]], [[1lou|1lou]], [[1qjh|1qjh]], [[1ris|1ris]], [[1twt|1twt]], [[2bvz|2bvz]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=2bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxj OCA], [http://pdbe.org/2bxj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bxj RCSB], [http://www.ebi.ac.uk/pdbsum/2bxj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bxj ProSAT]</span></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=2bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxj OCA], [https://pdbe.org/2bxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bxj RCSB], [https://www.ebi.ac.uk/pdbsum/2bxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bxj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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). | + | [https://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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Otzen, D E]] | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Ribosomal protein]] | + | [[Category: Otzen DE]] |
| - | [[Category: Rna-binding]]
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| - | [[Category: S6 double mutant]]
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| Structural highlights
Function
RS6_THETH Located on the outer edge of the platform on the body of the 30S subunit (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
When folding to the native state N in the presence of salt, the apparent two-state folder S6 transiently forms a transient off-pathway state C with substantial secondary and tertiary structure. Fifteen double mutant cycles were analysed to compare side-chain interaction energies DeltaDeltaG(int) in C, N and TS (the transition state between N and the denatured state). The kinetic signatures of these destabilizing mutants suggest folding scenarios involving unfolding intermediates and even alternative unfolding pathways. However, restricting the kinetic data to linear parts of the chevron plot allows reliable extrapolation to zero molar denaturant of rate constants of folding, unfolding and misfolding. Side-chain interactions appear to contribute to the stability of C, but in a substantially non-native environment, as shown by changes in the sign of DeltaDeltaG(int) between C and N. Remarkably, there appear to be significant (0.7-2 kcal/mol) antagonistic interactions between the two residues Leu30 and Leu75 in N and TS, which may be linked to subtle structural changes seen in the crystal structures of the mutants. A small number of overlapping residues are involved in these kinds of antagonistic interactions in N, TS and C, suggesting that repulsive interactions are coded into the protein topology whether the protein folds or misfolds. Destabilizing double mutants indicate that apparent two-state folders can be induced to behave in more complex ways provided that the native state is suitably destabilized.
Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis.,Otzen D Protein Eng Des Sel. 2005 Nov;18(11):547-57. Epub 2005 Oct 17. PMID:16230299[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Otzen D. Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis. Protein Eng Des Sel. 2005 Nov;18(11):547-57. Epub 2005 Oct 17. PMID:16230299 doi:10.1093/protein/gzi063
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