1mas

From Proteopedia

Revision as of 13:38, 30 October 2007

PURINE NUCLEOSIDE HYDROLASE

Overview

Protozoan parasites rely on the host for purines since they lack a de novo, synthetic pathway. Crithidia fasciculata salvages exogenous inosine, primarily through hydrolysis of the N-ribosidic bond using several, nucleoside hydrolases. The most abundant nucleoside hydrolase is, relatively nonspecific but prefers inosine and uridine as substrates. Here, we report the three-dimensional structure of the inosine-uridine, nucleoside hydrolase (IU-NH) from C. fasciculata determined by X-ray, crystallography at a nominal resolution of 2.5 A. The enzyme has an open, (alpha, beta) structure which differs from the classical dinucleotide, binding fold. IU-nucleoside hydrolase is composed of a mixed, eight-stranded beta sheet surrounded by six alpha helices and a small, C-terminal lobe composed of ... [(full description)]

About this Structure

1MAS is a [Single protein] structure of sequence from [Crithidia fasciculata] with K as [ligand]. Active as [Purine nucleosidase], with EC number [3.2.2.1]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].

Reference

Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata., Degano M, Gopaul DN, Scapin G, Schramm VL, Sacchettini JC, Biochemistry. 1996 May 14;35(19):5971-81. PMID:8634238

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