Structure of pteridine reductase (PTR1) fromLeishmania tarentolae
| Autor: | Ming Zhao, Haiyan Zhao, David A. Matthews, Kottayil I. Varughese, Rose Ann Ferre, Tom Bray, John M. Whiteley, Marc Ouellette |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Protozoan Proteins Crystal structure Crystallography X-Ray Tetramer Structural Biology Oxidoreductase Animals Molecule Amino Acid Sequence Leishmania chemistry.chemical_classification biology Active site General Medicine biology.organism_classification Pteridine reductase Crystallography Enzyme chemistry biology.protein Oxidoreductases Sequence Alignment NADP |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 59:1539-1544 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444903013131 |
| Popis: | The protozoan parasites Leishmania utilize a pteridine-reducing enzyme, pteridine reductase (PTR1), to bypass antifolate inhibition. The crystal structure of PTR1 from L. tarentolae has been solved as a binary complex with NADPH at 2.8 A resolution. The structure was solved by molecular-replacement techniques using the recently reported L. major PTR1 structure as a search model. Comparisons of the present structure with the L. major PTR1 allowed us to identify regions of flexibility in the molecule. PTR1 is a member of the growing family of short-chain dehydrogenases (SDR) which share the characteristic Tyr(Xaa)(3)Lys motif in the vicinity of the active site. The functional enzyme is a tetramer and the crystallographic asymmetric unit contains a tetramer with 222 point-group symmetry. |
| Databáze: | OpenAIRE |
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