1sar: Difference between revisions

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New page: left|200px<br /><applet load="1sar" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sar, resolution 1.8Å" /> '''DETERMINATION AND RES...
 
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[[Image:1sar.jpg|left|200px]]<br /><applet load="1sar" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sar, resolution 1.8&Aring;" />
'''DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION'''<br />


==Overview==
==DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION==
The crystal structures of ribonuclease from Streptomyces aureofaciens, (RNase Sa) and its complex with 3'-guanylic acid (guanosine, 3'-monophosphate, 3'-GMP) have been determined by the method of, isomorphous replacement. The atomic parameters have been refined by, restrained least-squares minimization using data in the resolution range, 10.0-1.8 A. All protein atoms and more than 230 water atoms in the two, crystal structures have been refined to crystallographic R factors of, 0.172 and 0.175 respectively. The estimated r.m.s. error in the atomic, positions ranges from 0.2 A for well-defined atoms to about 0.5 A for more, poorly defined atoms. There are two enzyme molecules in the asymmetric, unit, built independently, and referred to as molecules A and B. The value, of the average B factor for protein atoms in both structures is about 19, A2 and for water molecules about 35 A2. Electron density for the substrate, analogue 3'-GMP was found only at the active site of molecule A. The, density was very clear and the positions of all 3'-GMP atoms were refined, with precision comparable to that of the protein.
<StructureSection load='1sar' size='340' side='right'caption='[[1sar]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sar]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SAR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sar OCA], [https://pdbe.org/1sar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sar RCSB], [https://www.ebi.ac.uk/pdbsum/1sar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sar ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
== 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/sa/1sar_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=1sar ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SAR OCA].
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8 A resolution., Sevcik J, Dodson EJ, Dodson GG, Acta Crystallogr B. 1991 Apr 1;47 ( Pt 2):240-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1654932 1654932]
[[Category: Kitasatospora aureofaciens]]
[[Category: Ribonuclease T(1)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Dodson EJ]]
[[Category: Streptomyces aureofaciens]]
[[Category: Dodson GG]]
[[Category: Dodson, E.J.]]
[[Category: Sevcik J]]
[[Category: Dodson, G.G.]]
[[Category: Sevcik, J.]]
[[Category: SO4]]
[[Category: hydrolase (endoribonuclease)]]
 
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