1fzu: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fzu.jpg|left|200px]]
- {{Structure
+==RNAse T1 V78A mutant==
-|PDB= 1fzu |SIZE=350|CAPTION= <scene name='initialview01'>1fzu</scene>, resolution 1.8&Aring;
+<StructureSection load='1fzu' size='340' side='right'caption='[[1fzu]], [[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&#39;-MONOPHOSPHATE'>2GP</scene>
+<table><tr><td colspan='2'>[[1fzu]] 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=1FZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZU 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=1fzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzu OCA], [https://pdbe.org/1fzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fzu RCSB], [https://www.ebi.ac.uk/pdbsum/1fzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fzu 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/fz/1fzu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fzu ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''RNAse T1 V78A mutant'''
+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:11513591<ref>PMID:11513591</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1fzu" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-FZU 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=1FZU OCA].
+__TOC__
+</StructureSection>
-==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: Ribonuclease T(1)]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[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: ribonuclease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:51:40 2008''