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[[Image:2aas.jpg|left|200px]]


{{Structure
==HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY==
|PDB= 2aas |SIZE=350|CAPTION= <scene name='initialview01'>2aas</scene>
<StructureSection load='2aas' size='340' side='right'caption='[[2aas]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2aas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AAS FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 32 models</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aas OCA], [https://pdbe.org/2aas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aas RCSB], [https://www.ebi.ac.uk/pdbsum/2aas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aas ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</ref>
== 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/aa/2aas_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=2aas ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
High-resolution three-dimensional structures of bovine pancreatic ribonuclease A in aqueous solution have been determined by nuclear magnetic resonance (NMR) spectroscopy combined with restrained molecular dynamics calculations. The structures are based on: (1) 464 interproton distance constraints with accurate upper and lower limits, determined from build-up rates of nuclear Overhauser effects (NOE) by using the complete relaxation matrix; (2) 999 more approximate upper limits for interproton distances; and (3) 42 dihedral angle constraints (37 for phi and 5 for chi 1). A total of 16 structures were calculated, which show a root-mean-square (r.m.s.) deviation of 0.66 A for the backbone atoms and 1.68 A for all heavy-atoms. The converged structures are highly similar to those found in the crystal state. r.m.s. deviation of backbone atom positions in the crystal as compared to those in the average solution structure is 0.92 A. Observed differences are concentrated in loop regions and in the neighborhood of His119 and His48 side-chains. Dynamic aspects, such as H/D amide proton exchange and side-chain mobility have been examined.


'''HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY'''
High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy.,Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J, Rico M J Mol Biol. 1993 Feb 5;229(3):722-34. PMID:8381876<ref>PMID:8381876</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2aas" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
High-resolution three-dimensional structures of bovine pancreatic ribonuclease A in aqueous solution have been determined by nuclear magnetic resonance (NMR) spectroscopy combined with restrained molecular dynamics calculations. The structures are based on: (1) 464 interproton distance constraints with accurate upper and lower limits, determined from build-up rates of nuclear Overhauser effects (NOE) by using the complete relaxation matrix; (2) 999 more approximate upper limits for interproton distances; and (3) 42 dihedral angle constraints (37 for phi and 5 for chi 1). A total of 16 structures were calculated, which show a root-mean-square (r.m.s.) deviation of 0.66 A for the backbone atoms and 1.68 A for all heavy-atoms. The converged structures are highly similar to those found in the crystal state. r.m.s. deviation of backbone atom positions in the crystal as compared to those in the average solution structure is 0.92 A. Observed differences are concentrated in loop regions and in the neighborhood of His119 and His48 side-chains. Dynamic aspects, such as H/D amide proton exchange and side-chain mobility have been examined.
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
== References ==
==About this Structure==
<references/>
2AAS is a [[Single protein]] structure of sequence 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=2AAS OCA].
__TOC__
 
</StructureSection>
==Reference==
High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy., Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J, Rico M, J Mol Biol. 1993 Feb 5;229(3):722-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8381876 8381876]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bruix M]]
[[Category: Bruix, M.]]
[[Category: Gonzalez C]]
[[Category: Gonzalez, C.]]
[[Category: Herranz J]]
[[Category: Herranz, J.]]
[[Category: Neira JL]]
[[Category: Neira, J L.]]
[[Category: Nieto JL]]
[[Category: Nieto, J L.]]
[[Category: Rico M]]
[[Category: Rico, M.]]
[[Category: Santoro J]]
[[Category: Santoro, J.]]
[[Category: hydrolase(endoribonuclease)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:30 2008''

Latest revision as of 10:33, 9 October 2024

HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPYHIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Structural highlights

2aas is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 32 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1]

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 PubMed

High-resolution three-dimensional structures of bovine pancreatic ribonuclease A in aqueous solution have been determined by nuclear magnetic resonance (NMR) spectroscopy combined with restrained molecular dynamics calculations. The structures are based on: (1) 464 interproton distance constraints with accurate upper and lower limits, determined from build-up rates of nuclear Overhauser effects (NOE) by using the complete relaxation matrix; (2) 999 more approximate upper limits for interproton distances; and (3) 42 dihedral angle constraints (37 for phi and 5 for chi 1). A total of 16 structures were calculated, which show a root-mean-square (r.m.s.) deviation of 0.66 A for the backbone atoms and 1.68 A for all heavy-atoms. The converged structures are highly similar to those found in the crystal state. r.m.s. deviation of backbone atom positions in the crystal as compared to those in the average solution structure is 0.92 A. Observed differences are concentrated in loop regions and in the neighborhood of His119 and His48 side-chains. Dynamic aspects, such as H/D amide proton exchange and side-chain mobility have been examined.

High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy.,Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J, Rico M J Mol Biol. 1993 Feb 5;229(3):722-34. PMID:8381876[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
  2. ↑ Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J, Rico M. High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy. J Mol Biol. 1993 Feb 5;229(3):722-34. PMID:8381876 doi:http://dx.doi.org/10.1006/jmbi.1993.1075
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