1j82

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1j82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j82, resolution 2.30&Aring;" /> '''Osmolyte Stabilizati...)
Current revision (07:50, 3 April 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1j82.jpg|left|200px]]<br /><applet load="1j82" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1j82, resolution 2.30&Aring;" />
 
-
'''Osmolyte Stabilization of RNase'''<br />
 
-
==Overview==
+
==Osmolyte Stabilization of RNase==
-
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.
+
<StructureSection load='1j82' size='340' side='right'caption='[[1j82]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
<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>
 +
</table>
 +
== Function ==
 +
[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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j8/1j82_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1J82 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 and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J82 OCA].
+
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11373282 11373282]
+
__TOC__
 +
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Pancreatic ribonuclease]]
+
[[Category: Large Structures]]
-
[[Category: Protein complex]]
+
[[Category: Ratnaparkhi GS]]
-
[[Category: Ratnaparkhi, G.S.]]
+
[[Category: Varadarajan R]]
-
[[Category: Varadarajan, R.]]
+
-
[[Category: NH2]]
+
-
[[Category: SO4]]
+
-
[[Category: betaine]]
+
-
[[Category: osmolyte soaking]]
+
-
[[Category: sarcosine]]
+
-
[[Category: taurine]]
+
-
[[Category: trimethylamine-n-oxide]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:00:16 2007''
+

Current revision

Osmolyte Stabilization of RNase

PDB ID 1j82

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j82"
Personal tools