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1mas

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{{STRUCTURE_1mas| PDB=1mas | SCENE= }}
{{STRUCTURE_1mas| PDB=1mas | SCENE= }}
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'''PURINE NUCLEOSIDE HYDROLASE'''
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===PURINE NUCLEOSIDE HYDROLASE===
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==Overview==
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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 four alpha helices. Two short antiparallel beta strands are involved in intermolecular contacts. The catalytic pocket is located at the C-terminal end of beta strands beta 1 and beta 4. Four aspartate residues are located at the bottom of the cavity in a geometry which suggests interaction with the ribose moiety of the nucleoside. These groups could provide the catalytically important interactions to the ribosyl hydroxyls and the stabilizing anion for the oxycarbonium-like transition state. Histidine 241, located on the side of the active site cavity, is the proposed proton donor which facilitates purine base departure [Gopaul, D. N., Meyer, S. L., Degano, M., Sacchettini, J. C., &amp; Schramm, V. L. (1996) Biochemistry 35, 5963-5970]. The substrate binding site is unlike that from purine nucleoside phosphorylase, phosphoribosyltransferases, or uracil DNA glycosylase and thus represents a novel architecture for general acid-base catalysis. This detailed knowledge of the architecture of the active site, together with the previous transition state analysis [Horenstein, B. A., Parkin, D. W., Estupinan, B., &amp; Schramm, V. L. (1991) Biochemistry 30, 10788-10795], allows analysis of the interactions leading to catalysis and an explanation for the tight-binding inhibitors of the enzyme [Schramm, V. L., Horenstein, B. A., &amp; Kline, P. C. (1994) J. Biol. Chem. 269, 18259-18262].
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{{ABSTRACT_PUBMED_8634238}}
==About this Structure==
==About this Structure==
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[[Category: Purine nucleosidase]]
[[Category: Purine nucleosidase]]
[[Category: Purine nucleoside hydrolase]]
[[Category: Purine nucleoside hydrolase]]
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Revision as of 20:34, 2 July 2008

Image:1mas.png

Template:STRUCTURE 1mas

PURINE NUCLEOSIDE HYDROLASE

Template:ABSTRACT PUBMED 8634238

About this Structure

1MAS is a Single protein structure of sequence from Crithidia fasciculata. 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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