1fev: Difference between revisions

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[[Image:1fev.gif|left|200px]]<br /><applet load="1fev" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fev.gif|left|200px]]
caption="1fev, resolution 2.25&Aring;" />
 
'''CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S'''<br />
{{Structure
|PDB= 1fev |SIZE=350|CAPTION= <scene name='initialview01'>1fev</scene>, resolution 2.25&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FEV 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 <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FEV OCA].  
1FEV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FEV OCA].  


==Reference==
==Reference==
Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S., Ratnaparkhi GS, Awasthi SK, Rani P, Balaram P, Varadarajan R, Protein Eng. 2000 Oct;13(10):697-702. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11112508 11112508]
Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S., Ratnaparkhi GS, Awasthi SK, Rani P, Balaram P, Varadarajan R, Protein Eng. 2000 Oct;13(10):697-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11112508 11112508]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
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[[Category: alpha aminoisobutyric acid]]
[[Category: alpha aminoisobutyric acid]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:58 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:08:11 2008''

Revision as of 12:08, 20 March 2008

File:1fev.gif


PDB ID 1fev

Drag the structure with the mouse to rotate
, resolution 2.25Å
Ligands:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S


OverviewOverview

The S protein-S peptide interaction is a model system to study binding thermodynamics in proteins. We substituted alanine at position 4 in S peptide by alpha-aminoisobutyric acid (Aib) to investigate the effect of this substitution on the conformation of free S peptide and on its binding to S protein. The thermodynamic consequences of this replacement were studied using isothermal titration calorimetry. The structures of the free and complexed peptides were studied using circular dichroic spectroscopy and X-ray crystallography, respectively. The alanine4Aib replacement stabilizes the free S peptide helix and does not perturb the tertiary structure of RNase S. Surprisingly, and in contrast to the wild-type S peptide, the DeltaG degrees of binding of peptide to S pro, over the temperature range 5-30 degrees C, is virtually independent of temperature. At 25 degrees C, the DeltaDeltaG degrees, DeltaDeltaH degrees, DeltaDeltaS and DeltaDeltaCp of binding are 0.7 kcal/mol, 2.8 kcal/mol, 6 kcal/mol x K and -60 kcal/mol x K, respectively. The positive value of DeltaDeltaS is probably due to a decrease in the entropy of uncomplexed alanine4Aib relative to the wild-type peptide. The positive value of DeltaDeltaH: degrees is unexpected and is probably due to favorable interactions formed in uncomplexed alanine4Aib. This study addresses the thermodynamic and structural consequences of a replacement of alanine by Aib both in the unfolded and complexed states in proteins.

About this StructureAbout this Structure

1FEV is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S., Ratnaparkhi GS, Awasthi SK, Rani P, Balaram P, Varadarajan R, Protein Eng. 2000 Oct;13(10):697-702. PMID:11112508

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