1c54
From Proteopedia
(New page: 200px<br /><applet load="1c54" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c54" /> '''SOLUTION STRUCTURE OF RIBONUCLEASE SA'''<br ...) |
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'''SOLUTION STRUCTURE OF RIBONUCLEASE SA'''<br /> | '''SOLUTION STRUCTURE OF RIBONUCLEASE SA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have used NMR methods to characterize the structure and dynamics of | + | 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== | ==About this Structure== | ||
| - | 1C54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Active as [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] Full crystallographic information is available from [http:// | + | 1C54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C54 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Streptomyces aureofaciens]] | [[Category: Streptomyces aureofaciens]] | ||
[[Category: Bruix, M.]] | [[Category: Bruix, M.]] | ||
| - | [[Category: Canadillas-Perez, J | + | [[Category: Canadillas-Perez, J M.]] |
| - | [[Category: Laurents, D | + | [[Category: Laurents, D V.]] |
| - | [[Category: Pace, C | + | [[Category: Pace, C N.]] |
[[Category: Rico, M.]] | [[Category: Rico, M.]] | ||
[[Category: Santoro, J.]] | [[Category: Santoro, J.]] | ||
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[[Category: alpha+beta protein]] | [[Category: alpha+beta protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:29 2008'' |
Revision as of 10:02, 21 February 2008
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SOLUTION STRUCTURE OF RIBONUCLEASE SA
Overview
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
1C54 is a Single protein structure of sequence from Streptomyces aureofaciens. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.
Reference
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
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