3FB1

Crystal Structure of Purine Nucleoside Phosphorylase in Complex with Ribose-1-Phosphate

3FB1 の概要

• エントリーDOI: 10.2210/pdb3fb1/pdb
• 関連するPDBエントリー: 1TCU 1TCV 1TD1 3F8W 3FAZ
• 分子名称: Purine-nucleoside phosphorylase, 1-O-phosphono-alpha-D-ribofuranose, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: purine nucleoside phsophorylase, ribose-1-phosphate, glycosyltransferase, transferase
• 由来する生物種: Schistosoma mansoni (Blood fluke)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 94459.22

構造登録者

Pereira, H.M.,Garratt, R.C.,Oliva, G. (登録日: 2008-11-18, 公開日: 2009-11-24, 最終更新日: 2023-12-27)

主引用文献

D'Muniz Pereira, H.,Oliva, G.,Garratt, R.C.
Purine nucleoside phosphorylase from Schistosoma mansoni in complex with ribose-1-phosphate.
J.Synchrotron Radiat., 18:62-65, 2011

PubMed Abstract: Schistosomes are blood flukes which cause schistosomiasis, a disease affecting approximately 200 million people worldwide. Along with several other important human parasites including trypanosomes and Plasmodium, schistosomes lack the de novo pathway for purine synthesis and depend exclusively on the salvage pathway for their purine requirements, making the latter an attractive target for drug development. Part of the pathway involves the conversion of inosine (or guanosine) into hypoxanthine (or guanine) together with ribose-1-phosphate (R1P) or vice versa. This inter-conversion is undertaken by the enzyme purine nucleoside phosphorylase (PNP) which has been used as the basis for the development of novel anti-malarials, conceptually validating this approach. It has been suggested that, during the reverse reaction, R1P binding to the enzyme would occur only as a consequence of conformational changes induced by hypoxanthine, thus making a binary PNP-R1P complex unlikely. Contradictory to this statement, a crystal structure of just such a binary complex involving the Schistosoma mansoni enzyme has been successfully obtained. The ligand shows an intricate hydrogen-bonding network in the phosphate and ribose binding sites and adds a further chapter to our knowledge which could be of value in the future development of selective inhibitors.

PubMed: 21169694
DOI: 10.1107/S0909049510027718

実験手法

X-RAY DIFFRACTION (2.002 Å)