3bn0: Difference between revisions

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 <StructureSection load='3bn0' size='340' side='right'caption='[[3bn0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3bn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BN0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3bn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BN0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1emw|1emw]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpsP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=3bn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bn0 OCA], [https://pdbe.org/3bn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bn0 RCSB], [https://www.ebi.ac.uk/pdbsum/3bn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bn0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RS16_AQUAE RS16_AQUAE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=3bn0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Understanding the mechanisms that dictate protein stability is of large relevance, for instance, to enable design of temperature-tolerant enzymes with high enzymatic activity over a broad temperature interval. In an effort to identify such mechanisms, we have performed a detailed comparative study of the folding thermodynamics and kinetics of the ribosomal protein S16 isolated from a mesophilic (S16(meso)) and hyperthermophilic (S16(thermo)) bacterium by using a variety of biophysical methods. As basis for the study, the 2.0 A X-ray structure of S16(thermo) was solved using single wavelength anomalous dispersion phasing. Thermal unfolding experiments yielded midpoints of 59 and 111 degrees C with associated changes in heat capacity upon unfolding (DeltaC(p)(0)) of 6.4 and 3.3 kJ mol(-1) K(-1), respectively. A strong linear correlation between DeltaC(p)(0) and melting temperature (T(m)) was observed for the wild-type proteins and mutated variants, suggesting that these variables are intimately connected. Stopped-flow fluorescence spectroscopy shows that S16(meso) folds through an apparent two-state model, whereas S16(thermo) folds through a more complex mechanism with a marked curvature in the refolding limb indicating the presence of a folding intermediate. Time-resolved energy transfer between Trp and N-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-yl)methyl iodoacetamide of proteins mutated at selected positions shows that the denatured state ensemble of S16(thermo) is more compact relative to S16(meso). Taken together, our results suggest the presence of residual structure in the denatured state ensemble of S16(thermo) that appears to account for the large difference in quantified DeltaC(p)(0) values and, in turn, parts of the observed extreme thermal stability of S16(thermo). These observations may be of general importance in the design of robust enzymes that are highly active over a wide temperature span.
-Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.,Wallgren M, Aden J, Pylypenko O, Mikaelsson T, Johansson LB, Rak A, Wolf-Watz M J Mol Biol. 2008 Jun 13;379(4):845-58. Epub 2008 Apr 8. PMID:18471828<ref>PMID:18471828</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3bn0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ribosomal protein S16|Ribosomal protein S16]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Aquifex aeolicus huber and stetter 2001]]
+[[Category: Aquifex aeolicus]]
 [[Category: Large Structures]]
-[[Category: Pylypenko, O]]
+[[Category: Pylypenko O]]
-[[Category: Rak, A]]
+[[Category: Rak A]]
-[[Category: Ribonucleoprotein]]
-[[Category: Ribosomal protein]]
-[[Category: Ribosome]]