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[[Image:1ch0.jpg|left|200px]]
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{{STRUCTURE_1ch0|  PDB=1ch0  |  SCENE=  }}
'''RNASE T1 VARIANT WITH ALTERED GUANINE BINDING SEGMENT'''


==RNASE T1 VARIANT WITH ALTERED GUANINE BINDING SEGMENT==
<StructureSection load='1ch0' size='340' side='right'caption='[[1ch0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ch0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CH0 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2GP:GUANOSINE-2-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=1ch0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ch0 OCA], [https://pdbe.org/1ch0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ch0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ch0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ch0 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/ch/1ch0_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=1ch0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ribonuclease T1 variant 9/5 with a guanine recognition segment, altered from the wild-type amino acid sequence 41-KYNNYE-46 to 41-EFRNWQ-46, has been cocrystallised with the specific inhibitor 2'-GMP. The crystal structure has been refined to a crystallographic R factor of 0.198 at 2.3 A resolution. Despite a size reduction of the binding pocket, pushing the inhibitor outside by 1 A, 2'-GMP is fixed to the primary recognition site due to increased aromatic stacking interactions. The phosphate group of 2'-GMP is located about 4.2 A apart from its position in wild-type ribonuclease T1-2'-GMP complexes, allowing a Ca(2+), coordinating this phosphate group, to enter the binding pocket. The crystallographic data can be aligned with the kinetic characterisation of the variant, showing a reduction of both, guanine affinity and turnover rate. The presence of Ca(2+) was shown to inhibit variant 9/5 and wild-type enzyme to nearly the same extent.


==Overview==
Structural analysis of an RNase T1 variant with an altered guanine binding segment.,Hoschler K, Hoier H, Hubner B, Saenger W, Orth P, Hahn U J Mol Biol. 1999 Dec 17;294(5):1231-8. PMID:10600381<ref>PMID:10600381</ref>
The ribonuclease T1 variant 9/5 with a guanine recognition segment, altered from the wild-type amino acid sequence 41-KYNNYE-46 to 41-EFRNWQ-46, has been cocrystallised with the specific inhibitor 2'-GMP. The crystal structure has been refined to a crystallographic R factor of 0.198 at 2.3 A resolution. Despite a size reduction of the binding pocket, pushing the inhibitor outside by 1 A, 2'-GMP is fixed to the primary recognition site due to increased aromatic stacking interactions. The phosphate group of 2'-GMP is located about 4.2 A apart from its position in wild-type ribonuclease T1-2'-GMP complexes, allowing a Ca(2+), coordinating this phosphate group, to enter the binding pocket. The crystallographic data can be aligned with the kinetic characterisation of the variant, showing a reduction of both, guanine affinity and turnover rate. The presence of Ca(2+) was shown to inhibit variant 9/5 and wild-type enzyme to nearly the same extent.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1CH0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CH0 OCA].
</div>
<div class="pdbe-citations 1ch0" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural analysis of an RNase T1 variant with an altered guanine binding segment., Hoschler K, Hoier H, Hubner B, Saenger W, Orth P, Hahn U, J Mol Biol. 1999 Dec 17;294(5):1231-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10600381 10600381]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus oryzae]]
[[Category: Aspergillus oryzae]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hahn, U.]]
[[Category: Hahn U]]
[[Category: Hoeschler, K.]]
[[Category: Hoeschler K]]
[[Category: Hoier, H.]]
[[Category: Hoier H]]
[[Category: Hubner, B.]]
[[Category: Hubner B]]
[[Category: Orth, P.]]
[[Category: Orth P]]
[[Category: Saenger, W.]]
[[Category: Saenger W]]
[[Category: Ribonuclease]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:43:30 2008''

Latest revision as of 05:51, 9 August 2023

RNASE T1 VARIANT WITH ALTERED GUANINE BINDING SEGMENT

1ch0, resolution 2.30Å

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