1kh8: Difference between revisions

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[[Image:1kh8.gif|left|200px]]


{{Structure
==Structure of a cis-proline (P114) to glycine variant of Ribonuclease A==
|PDB= 1kh8 |SIZE=350|CAPTION= <scene name='initialview01'>1kh8</scene>, resolution 2.0&Aring;
<StructureSection load='1kh8' size='340' side='right'caption='[[1kh8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1kh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KH8 FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kh8 OCA], [https://pdbe.org/1kh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kh8 RCSB], [https://www.ebi.ac.uk/pdbsum/1kh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kh8 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kh8 OCA], [http://www.ebi.ac.uk/pdbsum/1kh8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kh8 RCSB]</span>
== 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/kh/1kh8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1kh8 ConSurf].
<div style="clear:both"></div>


'''Structure of a cis-proline (P114) to glycine variant of Ribonuclease A'''
==See Also==
 
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
== References ==
==Overview==
<references/>
Replacement of a cis-proline by glycine at position 114 in ribonuclease A leads to a large decrease in thermal stability and simplifies the refolding kinetics. A crystallographic approach was used to determine whether the decrease in thermal stability results from the presence of a cis glycine peptide bond, or from a localized structural rearrangement caused by the isomerization of the mutated cis 114 peptide bond. The structure was solved at 2.0 A resolution and refined to an R-factor of 19.5% and an R(free) of 21.9%. The overall conformation of the protein was similar to that of wild-type ribonuclease A; however, there was a large localized rearrangement of the mutated loop (residues 110-117-a 9.3 A shift of the Calpha atom of residue 114). The peptide bond before Gly114 is in the trans configuration. Interestingly, a large anomalous difference density was found near residue 114, and was attributed to a bound cesium ion present in the crystallization experiment. The trans isomeric configuration of the peptide bond in the folded state of this mutant is consistent with the refolding kinetics previously reported, and the associated protein conformational change provides an explanation for the decreased thermal stability.
__TOC__
 
</StructureSection>
==About this Structure==
1KH8 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=1KH8 OCA].
 
==Reference==
The crystal structure of the cis-proline to glycine variant (P114G) of ribonuclease A., Schultz DA, Friedman AM, White MA, Fox RO, Protein Sci. 2005 Nov;14(11):2862-70. Epub 2005 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16199662 16199662]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Fox RO]]
[[Category: Fox, R O.]]
[[Category: Friedman AM]]
[[Category: Friedman, A M.]]
[[Category: Schultz DA]]
[[Category: Schultz, D A.]]
[[Category: White MA]]
[[Category: White, M A.]]
[[Category: cesium]]
[[Category: cis]]
[[Category: proline]]
[[Category: ribonuclease some]]
[[Category: rnase some]]
[[Category: tran]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:32 2008''

Latest revision as of 09:05, 3 April 2024

Structure of a cis-proline (P114) to glycine variant of Ribonuclease AStructure of a cis-proline (P114) to glycine variant of Ribonuclease A

Structural highlights

1kh8 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
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.

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

1kh8, resolution 2.00Å

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