1P33

Pteridine reductase from Leishmania tarentolae complex with NADPH and MTX

1P33 の概要

• エントリーDOI: 10.2210/pdb1p33/pdb
• 関連するPDBエントリー: 1E7w 1E92
• 分子名称: Pteridine reductase 1, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, METHOTREXATE, ... (4 entities in total)
• 機能のキーワード: pteridine reductase, complex, nadph, mtx, oxidoreductase
• 由来する生物種: Leishmania tarentolae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 127890.50

構造登録者

Zhao, H.,Bray, T.,Ouellette, M.,Zhao, M.,Ferre, R.A.,Matthews, D.,Whiteley, J.M.,Varughese, K.I. (登録日: 2003-04-16, 公開日: 2003-09-02, 最終更新日: 2023-08-16)

主引用文献

Zhao, H.,Bray, T.,Ouellette, M.,Zhao, M.,Ferre, R.A.,Matthews, D.,Whiteley, J.M.,Varughese, K.I.
Structure of pteridine reductase (PTR1) from Leishmania tarentolae.
Acta Crystallogr.,Sect.D, 59:1539-1544, 2003

PubMed Abstract: 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.

PubMed: 12925782
DOI: 10.1107/S0907444903013131

実験手法

X-RAY DIFFRACTION (2.86 Å)