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New page: left|200px<br /><applet load="1iyy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iyy" /> '''NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 S...
 
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[[Image:1iyy.jpg|left|200px]]<br /><applet load="1iyy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1iyy" />
'''NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES'''<br />


==Overview==
==NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES==
Ribonuclease (RNase) T1 is a guanyloribonuclease, having two isozymes in, nature, Gln25- and Lys25-RNase T1. Between these two isozymes, there is no, difference in catalytic activity and three-dimensional structure; however, Lys25-RNase T1 is slightly more stable than Gln25-RNase T1. Recently, it, has been suggested that the existence of a salt bridge between Lys25 and, Asp29/Glu31 in Lys25-RNase T1 contributes to the stability. To elucidate, the effects of the replacement of Lys25 with a Gln on the conformation and, microenvironments of RNase T1 in detail, the three-dimensional solution, structure of Gln25-RNase T1 was determined by simulated-annealing, calculations. As a result, the topology of the overall folding was shown, to be very similar to that of the Lys25-isozyme except for some, differences. In particular, there were two differences in the property of, torsion angles of the two disulfide bonds and the conformations of the, residues 11-13, 63-66, and 92-93. With regard to the residues 11-13, the, lack of the above-mentioned salt bridge in Gln25-RNase T1 was thought to, induce the conformational difference of this segment as compared with the, Lys25-isozyme. Furthermore, it was proposed that the perturbation of this, segment might transfer to the residues 92-93 via the two disulfide bonds.
<StructureSection load='1iyy' size='340' side='right'caption='[[1iyy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iyy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1iyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyy OCA], [https://pdbe.org/1iyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyy RCSB], [https://www.ebi.ac.uk/pdbsum/1iyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNT1_ASPOR RNT1_ASPOR]
== 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/iy/1iyy_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=1iyy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribonuclease (RNase) T1 is a guanyloribonuclease, having two isozymes in nature, Gln25- and Lys25-RNase T1. Between these two isozymes, there is no difference in catalytic activity and three-dimensional structure; however, Lys25-RNase T1 is slightly more stable than Gln25-RNase T1. Recently, it has been suggested that the existence of a salt bridge between Lys25 and Asp29/Glu31 in Lys25-RNase T1 contributes to the stability. To elucidate the effects of the replacement of Lys25 with a Gln on the conformation and microenvironments of RNase T1 in detail, the three-dimensional solution structure of Gln25-RNase T1 was determined by simulated-annealing calculations. As a result, the topology of the overall folding was shown to be very similar to that of the Lys25-isozyme except for some differences. In particular, there were two differences in the property of torsion angles of the two disulfide bonds and the conformations of the residues 11-13, 63-66, and 92-93. With regard to the residues 11-13, the lack of the above-mentioned salt bridge in Gln25-RNase T1 was thought to induce the conformational difference of this segment as compared with the Lys25-isozyme. Furthermore, it was proposed that the perturbation of this segment might transfer to the residues 92-93 via the two disulfide bonds.


==About this Structure==
Determination of the NMR structure of Gln25-ribonuclease T1.,Hatano K, Kojima M, Suzuki E, Tanokura M, Takahashi K Biol Chem. 2003 Aug;384(8):1173-83. PMID:12974386<ref>PMID:12974386</ref>
1IYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. 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=1IYY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Determination of the NMR structure of Gln25-ribonuclease T1., Hatano K, Kojima M, Suzuki E, Tanokura M, Takahashi K, Biol Chem. 2003 Aug;384(8):1173-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12974386 12974386]
</div>
<div class="pdbe-citations 1iyy" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus oryzae]]
[[Category: Aspergillus oryzae]]
[[Category: Ribonuclease T(1)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Hatano K]]
[[Category: Hatano, K.]]
[[Category: Kojima M]]
[[Category: Kojima, M.]]
[[Category: Suzuki E]]
[[Category: Suzuki, E.]]
[[Category: Takahashi K]]
[[Category: Takahashi, K.]]
[[Category: Tanokura M]]
[[Category: Tanokura, M.]]
[[Category: endonuclease]]
[[Category: endoribonuclease]]
[[Category: ribonuclease]]
 
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Latest revision as of 23:39, 27 December 2023

NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES

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