3iom: Difference between revisions

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[[Image:3iom.png|left|200px]]
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{{STRUCTURE_3iom|  PDB=3iom  |  SCENE=  }}  
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===Crystal structure of Purine Nucleoside Phosphorylase from Mycobacterium tuberculosis in complex with 2'-Deoxyguanosine===
===Crystal structure of Purine Nucleoside Phosphorylase from Mycobacterium tuberculosis in complex with 2'-Deoxyguanosine===
{{ABSTRACT_PUBMED_20570524}}


 
==Function==
<!--
[[http://www.uniprot.org/uniprot/PUNA_MYCTU PUNA_MYCTU]] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine (By similarity).
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{{ABSTRACT_PUBMED_20570524}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:020570524</ref><references group="xtra"/>
<ref group="xtra">PMID:020570524</ref><references group="xtra"/><references/>
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Purine-nucleoside phosphorylase]]
[[Category: Purine-nucleoside phosphorylase]]

Revision as of 11:42, 24 April 2013

Template:STRUCTURE 3iom

Crystal structure of Purine Nucleoside Phosphorylase from Mycobacterium tuberculosis in complex with 2'-Deoxyguanosine

Template:ABSTRACT PUBMED 20570524

Function

[PUNA_MYCTU] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine (By similarity).

About this Structure

3iom is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

  1. Ducati RG, Basso LA, Santos DS, de Azevedo WF Jr. Crystallographic and docking studies of purine nucleoside phosphorylase from Mycobacterium tuberculosis. Bioorg Med Chem. 2010 May 10. PMID:20570524 doi:10.1016/j.bmc.2010.05.009

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