|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2vup' size='340' side='right'caption='[[2vup]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2vup' size='340' side='right'caption='[[2vup]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vup]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_(trypanozoon)_brucei Trypanosoma (trypanozoon) brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VUP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VUP FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_peroxidase Glutathione peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.9 1.11.1.9] </span></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]] 2.1Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vup OCA], [http://pdbe.org/2vup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vup RCSB], [http://www.ebi.ac.uk/pdbsum/2vup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vup ProSAT]</span></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=2vup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vup OCA], [https://pdbe.org/2vup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vup RCSB], [https://www.ebi.ac.uk/pdbsum/2vup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vup ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q869A6_9TRYP Q869A6_9TRYP] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutathione peroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alphey, M S]] | + | [[Category: Trypanosoma brucei]] |
| - | [[Category: Fairlamb, A H]] | + | [[Category: Alphey MS]] |
| - | [[Category: Konig, J]] | + | [[Category: Fairlamb AH]] |
| - | [[Category: Dithiol-dependant peroxidase]] | + | [[Category: Konig J]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| - | [[Category: Trypanosoma]]
| + | |
| - | [[Category: Trypanothione]]
| + | |
| Structural highlights
Function
Q869A6_9TRYP
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
TbTDPX (Trypanosoma brucei tryparedoxin-dependent peroxidase) is a genetically validated drug target in the fight against African sleeping sickness. Despite its similarity to members of the GPX (glutathione peroxidase) family, TbTDPX2 is functional as a monomer, lacks a selenocysteine residue and relies instead on peroxidatic and resolving cysteine residues for catalysis and uses tryparedoxin rather than glutathione as electron donor. Kinetic studies indicate a saturable Ping Pong mechanism, unlike selenium-dependent GPXs, which display infinite K(m) and V(max) values. The structure of the reduced enzyme at 2.1 A (0.21 nm) resolution reveals that the catalytic thiol groups are widely separated [19 A (0.19 nm)] and thus unable to form a disulphide bond without a large conformational change in the secondary-structure architecture, as reported for certain plant GPXs. A model of the oxidized enzyme structure is presented and the implications for small-molecule inhibition are discussed.
Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases.,Alphey MS, Konig J, Fairlamb AH Biochem J. 2008 Sep 15;414(3):375-81. PMID:18522537[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alphey MS, Konig J, Fairlamb AH. Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases. Biochem J. 2008 Sep 15;414(3):375-81. PMID:18522537 doi:10.1042/BJ20080889
|
