2XOX

Crystal structure of pteridine reductase (PTR1) from Leishmania donovani

2XOX の概要

• エントリーDOI: 10.2210/pdb2xox/pdb
• 分子名称: PTERIDINE REDUCTASE, SULFATE ION (3 entities in total)
• 機能のキーワード: oxidoreductase, antifolates, short-chain reductase
• 由来する生物種: LEISHMANIA DONOVANI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60753.07

構造登録者

Barrack, K.L.,Tulloch, L.B.,Burke, L.A.,Fyfe, P.K.,Hunter, W.N. (登録日: 2010-08-24, 公開日: 2011-01-12, 最終更新日: 2023-12-20)

主引用文献

Barrack, K.L.,Tulloch, L.B.,Burke, L.A.,Fyfe, P.K.,Hunter, W.N.
Structure of Recombinant Leishmania Donovani Pteridine Reductase Reveals a Disordered Active Site.
Acta Crystallogr.,Sect.F, 67:33-, 2011

PubMed Abstract: Pteridine reductase (PTR1) is a potential target for drug development against parasitic Trypanosoma and Leishmania species, protozoa that are responsible for a range of serious diseases found in tropical and subtropical parts of the world. As part of a structure-based approach to inhibitor development, specifically targeting Leishmania species, well ordered crystals of L. donovani PTR1 were sought to support the characterization of complexes formed with inhibitors. An efficient system for recombinant protein production was prepared and the enzyme was purified and crystallized in an orthorhombic form with ammonium sulfate as the precipitant. Diffraction data were measured to 2.5 Å resolution and the structure was solved by molecular replacement. However, a sulfate occupies a phosphate-binding site used by NADPH and occludes cofactor binding. The nicotinamide moiety is a critical component of the active site and without it this part of the structure is disordered. The crystal form obtained under these conditions is therefore unsuitable for the characterization of inhibitor complexes.

PubMed: 21206018
DOI: 10.1107/S174430911004724X

実験手法

X-RAY DIFFRACTION (2.5 Å)