1mas: Difference between revisions

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New page: left|200px<br /> <applet load="1mas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mas, resolution 2.5Å" /> '''PURINE NUCLEOSIDE HY...
 
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==About this Structure==
==About this Structure==
1MAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]] with K as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.1 3.2.2.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MAS OCA]].  
1MAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]] with K as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Purine_nucleosidase Purine nucleosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.1 3.2.2.1]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MAS OCA]].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8634238 8634238]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8634238 8634238]
[[Category: Crithidia fasciculata]]
[[Category: Crithidia fasciculata]]
[[Category: Purine nucleosidase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Degano, M.]]
[[Category: Degano, M.]]
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[[Category: purine nucleoside hydrolase]]
[[Category: purine nucleoside hydrolase]]


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Revision as of 13:04, 30 October 2007

File:1mas.gif


1mas, resolution 2.5Å

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PURINE NUCLEOSIDE HYDROLASE

OverviewOverview

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 StructureAbout 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].

ReferenceReference

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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OCA