6gxg: 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: @@
-'''Unreleased structure'''
-The entry 6gxg is ON HOLD
+==Tryparedoxin from Trypanosoma brucei in complex with CFT==
+<StructureSection load='6gxg' size='340' side='right'caption='[[6gxg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6gxg]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Trybb Trybb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GXG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GXG FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FFN:5-(4-fluorophenyl)-2-methyl-3~{H}-thieno[2,3-d]pyrimidin-4-one'>FFN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gxg OCA], [http://pdbe.org/6gxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gxg RCSB], [http://www.ebi.ac.uk/pdbsum/6gxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gxg ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TYPX_TRYBB TYPX_TRYBB]] Acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Trypanosomal and leishmanial infections claim tens of thousands of lives each year. The metabolism of these single cell eukaryotic parasites differs from the human host and their enzymes thus constitute promising drug targets. Tryparedoxin (Tpx) from Trypanosoma brucei is the essential oxidoreductase in the parasite's hydroperoxide clearance cascade. Functional in vitro and in vivo assays show that a small, selective inhibitor efficiently inhibits Tpx. By X-ray crystallography, SAXS, analytical SEC, SEC-MALS, MD simulations, ITC, and NMR spectroscopy, we show how covalent binding of this monofunctional inhibitor leads to Tpx dimerization. Intra- and intermolecular inhibitor-inhibitor, protein-protein and inhibitor-protein interactions stabilize the dimer. The behavior of this efficient antitrypanosomal molecule thus constitutes an exquisite example of chemically induced dimerization with a small, monovalent ligand that can be exploited for future drug design.
-Authors:
+Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes.,Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA Angew Chem Int Ed Engl. 2019 Jan 3. doi: 10.1002/anie.201810470. PMID:30605929<ref>PMID:30605929</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6gxg" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Trybb]]
+[[Category: Bader, N]]
+[[Category: Hellmich, U]]
+[[Category: Schindelin, H]]
+[[Category: Wagner, A]]
+[[Category: Covalent inhibitor]]
+[[Category: Inhibitor-induced dimerization]]
+[[Category: Monomer-dimer mixture]]
+[[Category: Oxidoreductase]]
+[[Category: Photoreduction]]