2VUP
Crystal structure of a type II tryparedoxin-dependant peroxidase from Trypanosoma brucei
Summary for 2VUP
| Entry DOI | 10.2210/pdb2vup/pdb |
| Descriptor | GLUTATHIONE PEROXIDASE-LIKE PROTEIN (2 entities in total) |
| Functional Keywords | oxidoreductase, peroxidase, trypanosoma, trypanothione, dithiol-dependant peroxidase |
| Biological source | TRYPANOSOMA BRUCEI |
| Total number of polymer chains | 1 |
| Total formula weight | 21139.06 |
| Authors | Alphey, M.S.,Konig, J.,Fairlamb, A.H. (deposition date: 2008-05-28, release date: 2008-06-17, Last modification date: 2023-12-13) |
| Primary citation | Alphey, M.S.,Konig, J.,Fairlamb, A.H. Structural and Mechanistic Insights Into Type II Trypanosomatid Tryparedoxin-Dependent Peroxidases. Biochem.J., 414:375-, 2008 Cited by PubMed Abstract: 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. PubMed: 18522537DOI: 10.1042/BJ20080889 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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