1i2g: Difference between revisions

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New page: left|200px<br /><applet load="1i2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i2g, resolution 1.85Å" /> '''Ribonuclease T1 V16T...
 
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[[Image:1i2g.jpg|left|200px]]<br /><applet load="1i2g" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1i2g, resolution 1.85&Aring;" />
'''Ribonuclease T1 V16T mutant'''<br />


==Overview==
==Ribonuclease T1 V16T mutant==
Differential scanning calorimetry, urea denaturation, and X-ray, crystallography were combined to study the structural and energetic, consequences of refilling an engineered cavity in the hydrophobic core of, RNase T1 with CH(3), SH, and OH groups. Three valines that cluster, together in the major hydrophobic core of T1 were each replaced with Ala, Ser, Thr, and Cys. Compared to the wild-type protein, all these mutants, reduce the thermodynamic stability of the enzyme considerably. The, relative order of stability at all three positions is as follows: Val &gt;, Ala approximately equal to Thr &gt; Ser. The effect of introducing a, sulfhydryl group is more variable. Surprisingly, a Val --&gt; Cys mutation in, a hydrophobic environment can be as or even more destabilizing than a Val, --&gt; Ser mutation. Furthermore, our results reveal that the penalty for, introducing an OH group into a hydrophobic cavity is roughly the same as, the gain obtained from filling the cavity with a CH(3) group. The inverse, equivalence of the behavior of hydroxyl and methyl groups seems to be, crucial for the unique three-dimensional structure of the proteins. The, importance of negative design elements in this context is highlighted.
<StructureSection load='1i2g' size='340' side='right'caption='[[1i2g]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i2g]] is a 1 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=1I2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I2G 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]] 1.85&#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></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=1i2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2g OCA], [https://pdbe.org/1i2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i2g RCSB], [https://www.ebi.ac.uk/pdbsum/1i2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i2g 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/i2/1i2g_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=1i2g ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1I2G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA and 2GP as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1I2G OCA].
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Hydrophobic core manipulations in ribonuclease T1., De Vos S, Backmann J, Prevost M, Steyaert J, Loris R, Biochemistry. 2001 Aug 28;40(34):10140-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11513591 11513591]
[[Category: Aspergillus oryzae]]
[[Category: Aspergillus oryzae]]
[[Category: Ribonuclease T(1)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Backmann J]]
[[Category: Backmann, J.]]
[[Category: De Vos S]]
[[Category: Loris, R.]]
[[Category: Loris R]]
[[Category: Steyaert, J.]]
[[Category: Steyaert J]]
[[Category: Vos, S.De.]]
[[Category: 2GP]]
[[Category: CA]]
[[Category: hydrophobic core packing]]
[[Category: ribonuclease t1]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:59:56 2007''

Latest revision as of 10:43, 3 April 2024

Ribonuclease T1 V16T mutantRibonuclease T1 V16T mutant

Structural highlights

1i2g is a 1 chain structure with sequence from Aspergillus oryzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNT1_ASPOR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1i2g, resolution 1.85Å

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