1i2e: Difference between revisions

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[[Image:1i2e.jpg|left|200px]]


{{Structure
==Ribonuclease T1 V16A mutant, form I==
|PDB= 1i2e |SIZE=350|CAPTION= <scene name='initialview01'>1i2e</scene>, resolution 1.8&Aring;
<StructureSection load='1i2e' size='340' side='right'caption='[[1i2e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=2GP:GUANOSINE-2'-MONOPHOSPHATE'>2GP</scene>
<table><tr><td colspan='2'>[[1i2e]] 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=1I2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I2E FirstGlance]. <br>
|ACTIVITY= [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]  
</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>
|GENE=  
<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=1i2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2e OCA], [https://pdbe.org/1i2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i2e RCSB], [https://www.ebi.ac.uk/pdbsum/1i2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i2e 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/i2/1i2e_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=1i2e ConSurf].
<div style="clear:both"></div>


'''Ribonuclease T1 V16A mutant, form I'''
==See Also==
 
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1I2E 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=1I2E OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/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: cavity creation]]
[[Category: hydrophobic core packing]]
[[Category: ribonuclease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:44:37 2008''

Latest revision as of 10:43, 3 April 2024

Ribonuclease T1 V16A mutant, form IRibonuclease T1 V16A mutant, form I

Structural highlights

1i2e 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 1.8Å
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

1i2e, resolution 1.80Å

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