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[[Image:1c54.jpg|left|200px]]
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{{STRUCTURE_1c54|  PDB=1c54  |  SCENE=  }}
'''SOLUTION STRUCTURE OF RIBONUCLEASE SA'''


==SOLUTION STRUCTURE OF RIBONUCLEASE SA==
<StructureSection load='1c54' size='340' side='right'caption='[[1c54]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c54]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C54 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1c54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c54 OCA], [https://pdbe.org/1c54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c54 RCSB], [https://www.ebi.ac.uk/pdbsum/1c54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c54 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
== 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/c5/1c54_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1c54 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have used NMR methods to characterize the structure and dynamics of ribonuclease Sa in solution. The solution structure of RNase Sa was obtained using the distance constraints provided by 2,276 NOEs and the C6-C96 disulfide bond. The 40 resulting structures are well determined; their mean pairwise RMSD is 0.76 A (backbone) and 1.26 A (heavy atoms). The solution structures are similar to previously determined crystal structures, especially in the secondary structure, but exhibit new features: the loop composed of Pro 45 to Ser 48 adopts distinct conformations and the rings of tyrosines 51, 52, and 55 have reduced flipping rates. Amide protons with greatly reduced exchange rates are found predominantly in interior beta-strands and the alpha-helix, but also in the external 3/10 helix and edge beta-strand linked by the disulfide bond. Analysis of (15)N relaxation experiments (R1, R2, and NOE) at 600 MHz revealed five segments, consisting of residues 1-5, 28-31, 46-50, 60-65, 74-77, retaining flexibility in solution. The change in conformation entropy for RNase SA folding is smaller than previously believed, since the native protein is more flexible in solution than in a crystal.


==Overview==
Solution structure and dynamics of ribonuclease Sa.,Laurents D, Perez-Canadillas JM, Santoro J, Rico M, Schell D, Pace CN, Bruix M Proteins. 2001 Aug 15;44(3):200-11. PMID:11455593<ref>PMID:11455593</ref>
We have used NMR methods to characterize the structure and dynamics of ribonuclease Sa in solution. The solution structure of RNase Sa was obtained using the distance constraints provided by 2,276 NOEs and the C6-C96 disulfide bond. The 40 resulting structures are well determined; their mean pairwise RMSD is 0.76 A (backbone) and 1.26 A (heavy atoms). The solution structures are similar to previously determined crystal structures, especially in the secondary structure, but exhibit new features: the loop composed of Pro 45 to Ser 48 adopts distinct conformations and the rings of tyrosines 51, 52, and 55 have reduced flipping rates. Amide protons with greatly reduced exchange rates are found predominantly in interior beta-strands and the alpha-helix, but also in the external 3/10 helix and edge beta-strand linked by the disulfide bond. Analysis of (15)N relaxation experiments (R1, R2, and NOE) at 600 MHz revealed five segments, consisting of residues 1-5, 28-31, 46-50, 60-65, 74-77, retaining flexibility in solution. The change in conformation entropy for RNase SA folding is smaller than previously believed, since the native protein is more flexible in solution than in a crystal.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1C54 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C54 OCA].
</div>
<div class="pdbe-citations 1c54" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solution structure and dynamics of ribonuclease Sa., Laurents D, Perez-Canadillas JM, Santoro J, Rico M, Schell D, Pace CN, Bruix M, Proteins. 2001 Aug 15;44(3):200-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11455593 11455593]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Streptomyces aureofaciens]]
<references/>
[[Category: Bruix, M.]]
__TOC__
[[Category: Canadillas-Perez, J M.]]
</StructureSection>
[[Category: Laurents, D V.]]
[[Category: Kitasatospora aureofaciens]]
[[Category: Pace, C N.]]
[[Category: Large Structures]]
[[Category: Rico, M.]]
[[Category: Bruix M]]
[[Category: Santoro, J.]]
[[Category: Canadillas-Perez JM]]
[[Category: Schell, D.]]
[[Category: Laurents DV]]
[[Category: Alpha+beta protein]]
[[Category: Pace CN]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:20:27 2008''
[[Category: Rico M]]
[[Category: Santoro J]]
[[Category: Schell D]]
Retrieved from "https://proteopedia.org/1c54"