1j82

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[[Image:1j82.jpg|left|200px]]
 
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{{Structure
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==Osmolyte Stabilization of RNase==
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|PDB= 1j82 |SIZE=350|CAPTION= <scene name='initialview01'>1j82</scene>, resolution 2.30&Aring;
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<StructureSection load='1j82' size='340' side='right'caption='[[1j82]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1j82]] 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=1J82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J82 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]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1j82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j82 OCA], [https://pdbe.org/1j82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j82 RCSB], [https://www.ebi.ac.uk/pdbsum/1j82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j82 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1j7z|1J7Z]], [[1j80|1J80]], [[1j81|1J81]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j82 OCA], [http://www.ebi.ac.uk/pdbsum/1j82 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j82 RCSB]</span>
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== Function ==
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}}
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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/j8/1j82_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=1j82 ConSurf].
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<div style="clear:both"></div>
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'''Osmolyte Stabilization of RNase'''
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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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==Overview==
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<references/>
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Osmolytes stabilize proteins to thermal and chemical denaturation. We have studied the effects of the osmolytes sarcosine, betaine, trimethylamine-N-oxide, and taurine on the structure and stability of the protein.peptide complex RNase S using x-ray crystallography and titration calorimetry, respectively. The largest degree of stabilization is achieved with 6 m sarcosine, which increases the denaturation temperatures of RNase S and S pro by 24.6 and 17.4 degrees C, respectively, at pH 5 and protects both proteins against tryptic cleavage. Four crystal structures of RNase S in the presence of different osmolytes do not offer any evidence for osmolyte binding to the folded state of the protein or any perturbation in the water structure surrounding the protein. The degree of stabilization in 6 m sarcosine increases with temperature, ranging from -0.52 kcal mol(-1) at 20 degrees C to -5.4 kcal mol(-1) at 60 degrees C. The data support the thesis that osmolytes that stabilize proteins, do so by perturbing unfolded states, which change conformation to a compact, folding competent state in the presence of osmolyte. The increased stabilization thus results from a decrease in conformational entropy of the unfolded state.
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__TOC__
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</StructureSection>
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==About this Structure==
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1J82 is a [[Protein complex]] structure of sequences 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=1J82 OCA].
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==Reference==
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Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states., Ratnaparkhi GS, Varadarajan R, J Biol Chem. 2001 Aug 3;276(31):28789-98. Epub 2001 May 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11373282 11373282]
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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: Protein complex]]
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[[Category: Ratnaparkhi GS]]
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[[Category: Ratnaparkhi, G S.]]
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[[Category: Varadarajan R]]
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[[Category: Varadarajan, R.]]
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[[Category: Betaine]]
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[[Category: Osmolyte soaking]]
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[[Category: Sarcosine]]
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[[Category: Taurine]]
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[[Category: Trimethylamine-n-oxide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Apr 5 19:11:12 2008''
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Current revision

Osmolyte Stabilization of RNase

PDB ID 1j82

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