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[[Image:1uck.jpg|left|200px]]
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{{STRUCTURE_1uck|  PDB=1uck  |  SCENE=  }}
'''Mutants of RNase Sa'''


==Mutants of RNase Sa==
<StructureSection load='1uck' size='340' side='right'caption='[[1uck]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1uck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UCK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1uck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uck OCA], [https://pdbe.org/1uck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uck RCSB], [https://www.ebi.ac.uk/pdbsum/1uck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uck ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uc/1uck_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1uck ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We previously suggested that proteins gain more stability from the burial and hydrogen bonding of polar groups than from the burial of nonpolar groups (Pace, C. N. (2001) Biochemistry 40, 310-313). To study this further, we prepared eight Thr-to-Val mutants of RNase Sa, four in which the Thr side chain is hydrogen-bonded and four in which it is not. We measured the stability of these mutants by analyzing their thermal denaturation curves. The four hydrogen-bonded Thr side chains contribute 1.3 +/- 0.9 kcal/mol to the stability; those that are not still contribute 0.4 +/- 0.9 kcal/mol to the stability. For 40 Thr-to-Val mutants of 11 proteins, the average decrease in stability is 1.0 +/- 1.0 kcal/mol when the Thr side chain is hydrogen-bonded and 0.0 +/- 0.5 kcal/mol when it is not. This is clear evidence that hydrogen bonds contribute favorably to protein stability. In addition, we prepared four Val-to-Thr mutants of RNase Sa, measured their stability, and determined their crystal structures. In all cases, the mutants are less stable than the wild-type protein, with the decreases in stability ranging from 0.5 to 4.4 kcal/mol. For 41 Val-to-Thr mutants of 11 proteins, the average decrease in stability is 1.8 +/- 1.3 kcal/mol and is unfavorable for 40 of 41 mutants. This shows that placing an [bond]OH group at a site designed for a [bond]CH3 group is very unfavorable. So, [bond]OH groups can contribute favorably to protein stability, even if they are not hydrogen-bonded, if the site was selected for an [bond]OH group, but they will make an unfavorable contribution to stability, even if they are hydrogen-bonded, when they are placed at a site selected for a [bond]CH3 group. The contribution that polar groups make to protein stability depends strongly on their environment.


==Overview==
The contribution of polar group burial to protein stability is strongly context-dependent.,Takano K, Scholtz JM, Sacchettini JC, Pace CN J Biol Chem. 2003 Aug 22;278(34):31790-5. Epub 2003 Jun 10. PMID:12799387<ref>PMID:12799387</ref>
We previously suggested that proteins gain more stability from the burial and hydrogen bonding of polar groups than from the burial of nonpolar groups (Pace, C. N. (2001) Biochemistry 40, 310-313). To study this further, we prepared eight Thr-to-Val mutants of RNase Sa, four in which the Thr side chain is hydrogen-bonded and four in which it is not. We measured the stability of these mutants by analyzing their thermal denaturation curves. The four hydrogen-bonded Thr side chains contribute 1.3 +/- 0.9 kcal/mol to the stability; those that are not still contribute 0.4 +/- 0.9 kcal/mol to the stability. For 40 Thr-to-Val mutants of 11 proteins, the average decrease in stability is 1.0 +/- 1.0 kcal/mol when the Thr side chain is hydrogen-bonded and 0.0 +/- 0.5 kcal/mol when it is not. This is clear evidence that hydrogen bonds contribute favorably to protein stability. In addition, we prepared four Val-to-Thr mutants of RNase Sa, measured their stability, and determined their crystal structures. In all cases, the mutants are less stable than the wild-type protein, with the decreases in stability ranging from 0.5 to 4.4 kcal/mol. For 41 Val-to-Thr mutants of 11 proteins, the average decrease in stability is 1.8 +/- 1.3 kcal/mol and is unfavorable for 40 of 41 mutants. This shows that placing an [bond]OH group at a site designed for a [bond]CH3 group is very unfavorable. So, [bond]OH groups can contribute favorably to protein stability, even if they are not hydrogen-bonded, if the site was selected for an [bond]OH group, but they will make an unfavorable contribution to stability, even if they are hydrogen-bonded, when they are placed at a site selected for a [bond]CH3 group. The contribution that polar groups make to protein stability depends strongly on their environment.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1UCK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCK OCA].
</div>
<div class="pdbe-citations 1uck" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The contribution of polar group burial to protein stability is strongly context-dependent., Takano K, Scholtz JM, Sacchettini JC, Pace CN, J Biol Chem. 2003 Aug 22;278(34):31790-5. Epub 2003 Jun 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12799387 12799387]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Streptomyces aureofaciens]]
<references/>
[[Category: Pace, C N.]]
__TOC__
[[Category: Sacchettini, J C.]]
</StructureSection>
[[Category: Scholtz, J M.]]
[[Category: Kitasatospora aureofaciens]]
[[Category: Takano, K.]]
[[Category: Large Structures]]
[[Category: Burial polar]]
[[Category: Pace CN]]
[[Category: Hydrogen bond]]
[[Category: Sacchettini JC]]
[[Category: Protein stability]]
[[Category: Scholtz JM]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:02:26 2008''
[[Category: Takano K]]
Retrieved from "https://proteopedia.org/1uck"