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3iom
From Proteopedia
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{{STRUCTURE_3iom| PDB=3iom | SCENE= }} | {{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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==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
Contents |
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
- 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
