1c54: Difference between revisions
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<StructureSection load='1c54' size='340' side='right' caption='[[1c54]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1c54' size='340' side='right' caption='[[1c54]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c54]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1c54]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10762 Atcc 10762]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C54 FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c54 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c54 RCSB], [http://www.ebi.ac.uk/pdbsum/1c54 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c54 OCA], [http://pdbe.org/1c54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c54 RCSB], [http://www.ebi.ac.uk/pdbsum/1c54 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1c54" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 10762]] | ||
[[Category: Bruix, M]] | [[Category: Bruix, M]] | ||
[[Category: Canadillas-Perez, J M]] | [[Category: Canadillas-Perez, J M]] | ||
Revision as of 04:48, 12 September 2015
SOLUTION STRUCTURE OF RIBONUCLEASE SASOLUTION STRUCTURE OF RIBONUCLEASE SA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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