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1ucl

From Proteopedia

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[[Image:1ucl.jpg|left|200px]]
 
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==Mutants of RNase Sa==
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The line below this paragraph, containing "STRUCTURE_1ucl", creates the "Structure Box" on the page.
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<StructureSection load='1ucl' size='340' side='right'caption='[[1ucl]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ucl]] 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=1UCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UCL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82&#8491;</td></tr>
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<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>
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{{STRUCTURE_1ucl| PDB=1ucl | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ucl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucl OCA], [https://pdbe.org/1ucl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ucl RCSB], [https://www.ebi.ac.uk/pdbsum/1ucl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ucl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uc/1ucl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ucl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Mutants of RNase Sa'''
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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>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1UCL 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=1UCL OCA].
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</div>
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<div class="pdbe-citations 1ucl" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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]
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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[[Category: Single protein]]
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== References ==
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[[Category: Streptomyces aureofaciens]]
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<references/>
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[[Category: Pace, C N.]]
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__TOC__
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[[Category: Sacchettini, J C.]]
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</StructureSection>
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[[Category: Scholtz, J M.]]
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[[Category: Kitasatospora aureofaciens]]
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[[Category: Takano, K.]]
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[[Category: Large Structures]]
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[[Category: Burial polar]]
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[[Category: Pace CN]]
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[[Category: Hydrogen bond]]
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[[Category: Sacchettini JC]]
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[[Category: Protein stability]]
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[[Category: Scholtz JM]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:02:34 2008''
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[[Category: Takano K]]

Current revision

Mutants of RNase Sa

PDB ID 1ucl

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