1nda: Difference between revisions

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 <StructureSection load='1nda' size='340' side='right'caption='[[1nda]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1nda]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1nda]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDA FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#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>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nda OCA], [https://pdbe.org/1nda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nda RCSB], [https://www.ebi.ac.uk/pdbsum/1nda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nda ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TYTR_TRYCR TYTR_TRYCR]] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
+[https://www.uniprot.org/uniprot/TYTR_TRYCR TYTR_TRYCR] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1nda ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The three-dimensional structure of trypanothione reductase (TR) (EC 1.6.4.8) from Trypanosoma cruzi has been solved at 0.33 nm resolution by molecular replacement using the structure of C. fasciculata TR as a starting model. Elucidation of the T. cruzi TR structure represents the first step in the rational design of a drug against Chagas' disease. The structure of T. cruzi TR is compared with those of C. fasciculata TR as well as human and E. coli glutathione reductase (GR). In the FAD-binding domain, TR has two insertions, each about 10 residues long, which do not occur in GR. The first one is a rigid loop stabilizing the position of helix 91-117 which is responsible for the wider active site of TR as compared to GR. The second insertion does not occur where it is predicted by sequence alignment; rather the residues extend three strands of the 4-stranded beta-sheet by one or two residues each. This increases the number of hydrogen bonds within the sheet structure. The structure of the NADPH.TR complex has been solved at 0.33 nm resolution. The nicotinamide ring is sandwiched between the flavin ring and the side chain of Phe-198 which undergoes the same conformational change upon coenzyme binding as Tyr-197 in GR. In addition to Arg-222 and Arg-228, which are conserved in TR and GR, Tyr-221--the last residue of the second beta-sheet strand of the beta alpha beta dinucleotide binding fold--is in hydrogen bonding distance to the 2' phosphate group of NADPH.
-The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state.,Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL Proteins. 1994 Feb;18(2):161-73. PMID:8159665<ref>PMID:8159665</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1nda" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Trypanothione reductase|Trypanothione reductase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Trycr]]
+[[Category: Trypanosoma cruzi]]
-[[Category: Kabsch, W]]
+[[Category: Kabsch W]]
-[[Category: Krauth-Siegel, R L]]
+[[Category: Krauth-Siegel RL]]
-[[Category: Lantwin, C B]]
+[[Category: Lantwin CB]]
-[[Category: Pai, E F]]
+[[Category: Pai EF]]
-[[Category: Schlichting, I]]
+[[Category: Schlichting I]]
-[[Category: Oxidoreductase]]