1cjr

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(New page: 200px<br /><applet load="1cjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjr, resolution 2.30&Aring;" /> '''X-RAY CRYSTALLOGRAPH...)
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[[Image:1cjr.gif|left|200px]]<br /><applet load="1cjr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cjr, resolution 2.30&Aring;" />
 
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'''X-RAY CRYSTALLOGRAPHIC STUDIES OF DENATURATION IN RIBONUCLEASE S'''<br />
 
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==Overview==
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==X-RAY CRYSTALLOGRAPHIC STUDIES OF DENATURATION IN RIBONUCLEASE S==
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In an attempt to view the onset of urea denaturation in ribonuclease we, have collected X-ray diffraction data on ribonuclease S crystals soaked in, 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals, were stabilized by glutaraldehyde crosslinking. We have also collected, data on ribonuclease S crystals at low pH in an attempt to study the onset, of pH denaturation. The resolution of the datasets range from 1.9 to 3.0, A. Analysis of the structures reveals an increase in disorder with, increasing urea concentration. In the 5 M urea structure, this increase in, disorder is apparent all over the structure but is larger in loop and, helical regions than in the beta strands. The low pH structure shows a, very similar pattern of increased disorder. In addition there is a major, change in the position of the main chain (&gt; 1 A) in the 65-72 turn region., This region has previously been shown to be involved in one of the initial, steps of unfolding in the reduction of ribonuclease A. Crystallographic, analyses in the presence of denaturant, when combined with controlled, crosslinking, can thus provide detailed structural information that is, related to the initial steps of unfolding in solution. Proteins, 1999;36:282-294.
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<StructureSection load='1cjr' size='340' side='right'caption='[[1cjr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cjr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJR 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]] 2.3&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjr OCA], [https://pdbe.org/1cjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjr RCSB], [https://www.ebi.ac.uk/pdbsum/1cjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjr 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/cj/1cjr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cjr 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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In an attempt to view the onset of urea denaturation in ribonuclease we have collected X-ray diffraction data on ribonuclease S crystals soaked in 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals were stabilized by glutaraldehyde crosslinking. We have also collected data on ribonuclease S crystals at low pH in an attempt to study the onset of pH denaturation. The resolution of the datasets range from 1.9 to 3.0 A. Analysis of the structures reveals an increase in disorder with increasing urea concentration. In the 5 M urea structure, this increase in disorder is apparent all over the structure but is larger in loop and helical regions than in the beta strands. The low pH structure shows a very similar pattern of increased disorder. In addition there is a major change in the position of the main chain (&gt; 1 A) in the 65-72 turn region. This region has previously been shown to be involved in one of the initial steps of unfolding in the reduction of ribonuclease A. Crystallographic analyses in the presence of denaturant, when combined with controlled crosslinking, can thus provide detailed structural information that is related to the initial steps of unfolding in solution. Proteins 1999;36:282-294.
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==About this Structure==
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X-ray crystallographic studies of the denaturation of ribonuclease S.,Ratnaparkhi GS, Varadarajan R Proteins. 1999 Aug 15;36(3):282-94. PMID:10409822<ref>PMID:10409822</ref>
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1CJR 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=1CJR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-ray crystallographic studies of the denaturation of ribonuclease S., Ratnaparkhi GS, Varadarajan R, Proteins. 1999 Aug 15;36(3):282-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10409822 10409822]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1cjr" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Ratnaparkhi, G.S.]]
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[[Category: Varadarajan, R.]]
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[[Category: SO4]]
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[[Category: crosslinking]]
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[[Category: denaturation]]
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[[Category: low ph]]
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[[Category: rnase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:31:08 2007''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Ratnaparkhi GS]]
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[[Category: Varadarajan R]]

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X-RAY CRYSTALLOGRAPHIC STUDIES OF DENATURATION IN RIBONUCLEASE S

PDB ID 1cjr

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