2rln: Difference between revisions

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[[Image:2rln.gif|left|200px]]<br /><applet load="2rln" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2rln.gif|left|200px]]<br /><applet load="2rln" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2rln, resolution 1.85Å" />

'''THERMODYNAMIC AND STRUCTURAL CONSEQUENCES OF CHANGING A SULPHUR ATOM TO A METHYLENE GROUP IN THE M13NLE MUTATION IN RIBONUCLEASE S'''<br />

==Overview==

Two fragments of pancreatic ribonuclease A, a truncated version of, S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give, a catalytically active complex. We have substituted the wild-type residue, at position 13, methionine (Met), with norleucine (Nle), where the only, covalent change is the replacement of the sulfur atom with a methylene, group. The thermodynamic parameters associated with the binding of this, variant to S-protein, determined by titration calorimetry in the, temperature range 10-40 degrees C, are reported and compared to values, previously reported [Varadarajan, R., Connelly, P. R., Sturtevant, J. M., & Richards, F. M. (1992) Biochemistry 31, 1421-1426] for other position 13, analogs. The differences in the free energy and enthalpy of binding, between the Met and Nle peptides are 0.6 and 7.9 kcal/mol at 25 degrees C, respectively. These differences are slightly larger than, but comparable, to, the differences in the values for the Met/Ile and Met/Leu pairs. The, structure of the mutant complex was determined to 1.85 A resolution and, refined to an R-factor of 17.4%. The structures of mutant and wild-type, complexes are practically identical although the Nle side chain has a, significantly higher average B-factor than the corresponding Met side, chain. In contrast, the B-factors of the atoms of the cage of residues, surrounding position 13 are all somewhat lower in the Nle variant than the, Met wild-type.(ABSTRACT TRUNCATED AT 250 WORDS)

Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex. We have substituted the wild-type residue at position 13, methionine (Met), with norleucine (Nle), where the only covalent change is the replacement of the sulfur atom with a methylene group. The thermodynamic parameters associated with the binding of this variant to S-protein, determined by titration calorimetry in the temperature range 10-40 degrees C, are reported and compared to values previously reported [Varadarajan, R., Connelly, P. R., Sturtevant, J. M., & Richards, F. M. (1992) Biochemistry 31, 1421-1426] for other position 13 analogs. The differences in the free energy and enthalpy of binding between the Met and Nle peptides are 0.6 and 7.9 kcal/mol at 25 degrees C, respectively. These differences are slightly larger than, but comparable to, the differences in the values for the Met/Ile and Met/Leu pairs. The structure of the mutant complex was determined to 1.85 A resolution and refined to an R-factor of 17.4%. The structures of mutant and wild-type complexes are practically identical although the Nle side chain has a significantly higher average B-factor than the corresponding Met side chain. In contrast, the B-factors of the atoms of the cage of residues surrounding position 13 are all somewhat lower in the Nle variant than the Met wild-type.(ABSTRACT TRUNCATED AT 250 WORDS)

==About this Structure==

2RLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2RLN OCA].

2RLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NH2:'>NH2</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLN OCA].

==Reference==

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[[Category: rna)]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:18 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2rln.gif|left|200px]]<br /><applet load="2rln" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2rln.gif|left|200px]]<br /><applet load="2rln" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2rln, resolution 1.85&Aring;" />
 '''THERMODYNAMIC AND STRUCTURAL CONSEQUENCES OF CHANGING A SULPHUR ATOM TO A METHYLENE GROUP IN THE M13NLE MUTATION IN RIBONUCLEASE S'''<br />
 ==Overview==
-Two fragments of pancreatic ribonuclease A, a truncated version of, S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give, a catalytically active complex. We have substituted the wild-type residue, at position 13, methionine (Met), with norleucine (Nle), where the only, covalent change is the replacement of the sulfur atom with a methylene, group. The thermodynamic parameters associated with the binding of this, variant to S-protein, determined by titration calorimetry in the, temperature range 10-40 degrees C, are reported and compared to values, previously reported [Varadarajan, R., Connelly, P. R., Sturtevant, J. M., &amp; Richards, F. M. (1992) Biochemistry 31, 1421-1426] for other position 13, analogs. The differences in the free energy and enthalpy of binding, between the Met and Nle peptides are 0.6 and 7.9 kcal/mol at 25 degrees C, respectively. These differences are slightly larger than, but comparable, to, the differences in the values for the Met/Ile and Met/Leu pairs. The, structure of the mutant complex was determined to 1.85 A resolution and, refined to an R-factor of 17.4%. The structures of mutant and wild-type, complexes are practically identical although the Nle side chain has a, significantly higher average B-factor than the corresponding Met side, chain. In contrast, the B-factors of the atoms of the cage of residues, surrounding position 13 are all somewhat lower in the Nle variant than the, Met wild-type.(ABSTRACT TRUNCATED AT 250 WORDS)
+Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex. We have substituted the wild-type residue at position 13, methionine (Met), with norleucine (Nle), where the only covalent change is the replacement of the sulfur atom with a methylene group. The thermodynamic parameters associated with the binding of this variant to S-protein, determined by titration calorimetry in the temperature range 10-40 degrees C, are reported and compared to values previously reported [Varadarajan, R., Connelly, P. R., Sturtevant, J. M., &amp; Richards, F. M. (1992) Biochemistry 31, 1421-1426] for other position 13 analogs. The differences in the free energy and enthalpy of binding between the Met and Nle peptides are 0.6 and 7.9 kcal/mol at 25 degrees C, respectively. These differences are slightly larger than, but comparable to, the differences in the values for the Met/Ile and Met/Leu pairs. The structure of the mutant complex was determined to 1.85 A resolution and refined to an R-factor of 17.4%. The structures of mutant and wild-type complexes are practically identical although the Nle side chain has a significantly higher average B-factor than the corresponding Met side chain. In contrast, the B-factors of the atoms of the cage of residues surrounding position 13 are all somewhat lower in the Nle variant than the Met wild-type.(ABSTRACT TRUNCATED AT 250 WORDS)
 ==About this Structure==
-RLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2RLN OCA].
+RLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NH2:'>NH2</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLN OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: rna)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:57:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:18 2008''