1rbx

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[[Image:1rbx.gif|left|200px]]
 
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{{Structure
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==RIBONUCLEASE A (E.C.3.1.27.5) CONTROL==
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|PDB= 1rbx |SIZE=350|CAPTION= <scene name='initialview01'>1rbx</scene>, resolution 1.69&Aring;
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<StructureSection load='1rbx' size='340' side='right'caption='[[1rbx]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1rbx]] is a 1 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=1RBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RBX FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span>
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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]] 1.69&#8491;</td></tr>
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|GENE=
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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=1rbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rbx OCA], [https://pdbe.org/1rbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rbx RCSB], [https://www.ebi.ac.uk/pdbsum/1rbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rbx ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rbx OCA], [http://www.ebi.ac.uk/pdbsum/1rbx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rbx RCSB]</span>
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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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}}
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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/rb/1rbx_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=1rbx 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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Virtually all studies of the protein-folding reaction add either heat, acid, or a chemical denaturant to an aqueous protein solution in order to perturb the protein structure. When chemical denaturants are used, very high concentrations are usually necessary to observe any change in protein structure. In a solution with such high denaturant concentrations, both the structure of the protein and the structure of the solvent around the protein can be altered. X-ray crystallography is the obvious experimental technique to probe both types of changes. In this paper, we report the crystal structures of dihydrofolate reductase with urea and of ribonuclease A with guanidinium chloride. These two classic denaturants have similar effects on the native structure of the protein. The most important change that occurs is a reduction in the overall thermal factor. These structures offer a molecular explanation for the reduction in mobility. Although the reduction is observed only with the native enzyme in the crystal, a similar decrease in mobility has also been observed in the unfolded state in solution (Makhatadze G, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study.
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'''RIBONUCLEASE A (E.C.3.1.27.5) CONTROL'''
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The effect of denaturants on protein structure.,Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK Protein Sci. 1997 Aug;6(8):1727-33. PMID:9260285<ref>PMID:9260285</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1rbx" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Virtually all studies of the protein-folding reaction add either heat, acid, or a chemical denaturant to an aqueous protein solution in order to perturb the protein structure. When chemical denaturants are used, very high concentrations are usually necessary to observe any change in protein structure. In a solution with such high denaturant concentrations, both the structure of the protein and the structure of the solvent around the protein can be altered. X-ray crystallography is the obvious experimental technique to probe both types of changes. In this paper, we report the crystal structures of dihydrofolate reductase with urea and of ribonuclease A with guanidinium chloride. These two classic denaturants have similar effects on the native structure of the protein. The most important change that occurs is a reduction in the overall thermal factor. These structures offer a molecular explanation for the reduction in mobility. Although the reduction is observed only with the native enzyme in the crystal, a similar decrease in mobility has also been observed in the unfolded state in solution (Makhatadze G, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study.
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1RBX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RBX OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The effect of denaturants on protein structure., Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK, Protein Sci. 1997 Aug;6(8):1727-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9260285 9260285]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Pancreatic ribonuclease]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Dunbar JLH]]
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[[Category: Dunbar, J L.H.]]
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[[Category: Farber GK]]
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[[Category: Farber, G K.]]
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[[Category: hydrolase (nucleic acid]]
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[[Category: rna)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:25:59 2008''
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Current revision

RIBONUCLEASE A (E.C.3.1.27.5) CONTROL

PDB ID 1rbx

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