3cty: Difference between revisions

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-{{Seed}}
-[[Image:3cty.jpg|left|200px]]
-<!--
+==Crystal structure of T. acidophilum thioredoxin reductase==
-The line below this paragraph, containing "STRUCTURE_3cty", creates the "Structure Box" on the page.
+<StructureSection load='3cty' size='340' side='right'caption='[[3cty]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3cty]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CTY FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-{{STRUCTURE_3cty|  PDB=3cty  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cty OCA], [https://pdbe.org/3cty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cty RCSB], [https://www.ebi.ac.uk/pdbsum/3cty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cty ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9HJI4_THEAC Q9HJI4_THEAC]
+== 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/ct/3cty_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=3cty ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thioredoxin reductases (TrxRs) regulate the intracellular redox environment by using NADPH to provide reducing equivalents for thioredoxins (Trxs). Here we present the cloning and biochemical characterization of a putative TrxR (Ta0984) and a putative Trx (Ta0866) from Thermoplasma acidophilum. Our data identify Ta0866 as a Trx through its capacity to reduce insulin and be reduced by Escherichia coli TrxR in a NADPH-dependent manner. Our data also establish Ta0984 as a TrxR due to its ability to reduce T. acidophilum Trx ( taTrx), although not in a NADPH- or NADH-dependent manner. To explore the apparent inability of taTrxR to use NADPH or NADH as a reductant, we carried out a complete electrochemical characterization, which suggests that redox potential is not the source of this nonreactivity [Hamill et al. (2008) Biochemistry 47, 9738-9746]. Turning to crystallographic analysis, a 2.35 A resolution structure of taTrxR, also presented here, shows that despite the overall structural similarity to the well-characterized TrxR from E. coli (RMSD 1.30 A (2) for chain A), the "NADPH binding pocket" is not conserved. E. coli TrxR residues implicated in NADPH binding, H175, R176, R177, and R181, have been substituted with E185, Y186, M187, and M191 in the ta protein. Thus, we have identified a Trx and TrxR protein system from T. acidophilum for which the TrxR shares overall structural and redox properties with other TrxRs but lacks the appropriate binding motif to use the standard NADPH reductant. Our discovery of a TrxR that does not use NADPH provides a new twist in redox regulation.
-===Crystal structure of T. acidophilum thioredoxin reductase===
+Thioredoxin reductase from Thermoplasma acidophilum: a new twist on redox regulation.,Hernandez HH, Jaquez OA, Hamill MJ, Elliott SJ, Drennan CL Biochemistry. 2008 Sep 16;47(37):9728-37. Epub 2008 Aug 22. PMID:18717593<ref>PMID:18717593</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3cty" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18717593}}, adds the Publication Abstract to the page
+*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18717593 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18717593}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-CTY is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTY OCA].
-==Reference==
-<ref group="xtra">PMID:18717593</ref><references group="xtra"/>
 [[Category: Thermoplasma acidophilum]]
-[[Category: Drennan, C L.]]
+[[Category: Drennan CL]]
-[[Category: Hernandez, H H.]]
+[[Category: Hernandez HH]]
-[[Category: Fad]]
-[[Category: Flavin]]
-[[Category: Flavoprotein]]
-[[Category: Oxidoreductase]]
-[[Category: Thioredoxin reductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 25 09:28:58 2009''