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1d5h

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(New page: 200px<br /><applet load="1d5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5h, resolution 2.25&Aring;" /> '''Rnase s(f8a). mutant...)
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[[Image:1d5h.gif|left|200px]]<br /><applet load="1d5h" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d5h, resolution 2.25&Aring;" />
 
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'''Rnase s(f8a). mutant ribonucleasE S.'''<br />
 
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==Overview==
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==Rnase s(f8a). mutant ribonucleasE S.==
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The hydrophobic effect is widely believed to be an important determinant, of protein stability. However, it is difficult to obtain unambiguous, experimental estimates of the contribution of the hydrophobic driving, force to the overall free energy of folding. Thermodynamic and structural, studies of large to small substitutions in proteins are the most direct, method of measuring this contribution. We have substituted the buried, residue Phe8 in RNase S with alanine, methionine, and norleucine. Binding, thermodynamics and structures were characterized by titration calorimetry, and crystallography, respectively. The crystal structures of the RNase S, F8A, F8M, and F8Nle mutants indicate that the protein tolerates the, changes without any main chain adjustments. The correlation of structural, and thermodynamic parameters associated with large to small substitutions, was analyzed for nine mutants of RNase S as well as 32 additional, cavity-containing mutants of T4 lysozyme, human lysozyme, and barnase., Such substitutions were typically found to result in negligible changes in, DeltaC(p)() and positive values of both DeltaDeltaH degrees and, DeltaDeltaS of folding. Enthalpic effects were dominant, and the sign of, DeltaDeltaS is the opposite of that expected from the hydrophobic effect., Values of DeltaDeltaG degrees and DeltaDeltaH degrees correlated better, with changes in packing parameters such as residue depth or occluded, surface than with the change in accessible surface area upon folding., These results suggest that the loss of packing interactions rather than, the hydrophobic effect is a dominant contributor to the observed, energetics for large to small substitutions. Hence, estimates of the, magnitude of the hydrophobic driving force derived from earlier mutational, studies are likely to be significantly in excess of the actual value.
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<StructureSection load='1d5h' size='340' side='right'caption='[[1d5h]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d5h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D5H FirstGlance]. <br>
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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]] 2.25&#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=SET:AMINOSERINE'>SET</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1d5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d5h OCA], [https://pdbe.org/1d5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d5h RCSB], [https://www.ebi.ac.uk/pdbsum/1d5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d5h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</ref>
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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/d5/1d5h_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=1d5h ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1D5H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D5H OCA].
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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==Reference==
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<references/>
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Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics., Ratnaparkhi GS, Varadarajan R, Biochemistry. 2000 Oct 10;39(40):12365-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11015216 11015216]
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Ratnaparkhi, G.S]]
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[[Category: Ratnaparkhi GS]]
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[[Category: Varadarajan, R.]]
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[[Category: Varadarajan R]]
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[[Category: SO4]]
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[[Category: rnase s mutant f8a cavity s protein s peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:01:19 2007''
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Current revision

Rnase s(f8a). mutant ribonucleasE S.

PDB ID 1d5h

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