1p33
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Pteridine reductase from Leishmania tarentolae complex with NADPH and MTX
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Structural highlights
FunctionPTR1_LEITA Exhibits a NADPH-dependent biopterin reductase activity. Has good activity with folate and significant activity with dihydrofolate and dihydrobiopterin, but not with quinonoid dihydrobiopterin. Confers resistance to methotrexate (MTX). 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 PubMedThe 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. Structure of pteridine reductase (PTR1) from Leishmania tarentolae.,Zhao H, Bray T, Ouellette M, Zhao M, Ferre RA, Matthews D, Whiteley JM, Varughese KI Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1539-44. Epub 2003, Aug 19. PMID:12925782[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||||||
This page was last modified 09:36, 16 August 2023.