1pr2
From Proteopedia
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- | [[Image:1pr2.jpg|left|200px]] | + | [[Image:1pr2.jpg|left|200px]] |
- | + | ||
- | '''Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-[2-deoxyribofuranosyl]-6-methylpurine and Phosphate/Sulfate''' | + | {{Structure |
+ | |PDB= 1pr2 |SIZE=350|CAPTION= <scene name='initialview01'>1pr2</scene>, resolution 2.3Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=MDR:9-(2-DEOXY-BETA-D-RIBOFURANOSYL)-6-METHYLPURINE'>MDR</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-[2-deoxyribofuranosyl]-6-methylpurine and Phosphate/Sulfate''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1PR2 is a [ | + | 1PR2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_and_escherichia_coli_o157:h7 Escherichia coli, and escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PR2 OCA]. |
==Reference== | ==Reference== | ||
- | Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase., Bennett EM, Li C, Allan PW, Parker WB, Ealick SE, J Biol Chem. 2003 Nov 21;278(47):47110-8. Epub 2003 Aug 21. PMID:[http:// | + | Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase., Bennett EM, Li C, Allan PW, Parker WB, Ealick SE, J Biol Chem. 2003 Nov 21;278(47):47110-8. Epub 2003 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12937174 12937174] |
[[Category: Escherichia coli, and escherichia coli o157:h7]] | [[Category: Escherichia coli, and escherichia coli o157:h7]] | ||
[[Category: Purine-nucleoside phosphorylase]] | [[Category: Purine-nucleoside phosphorylase]] | ||
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[[Category: protein-nucleoside complex]] | [[Category: protein-nucleoside complex]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:00 2008'' |
Revision as of 11:28, 20 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | and | ||||||
Activity: | Purine-nucleoside phosphorylase, with EC number 2.4.2.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-[2-deoxyribofuranosyl]-6-methylpurine and Phosphate/Sulfate
Overview
Purine nucleoside phosphorylase catalyzes reversible phosphorolysis of purine nucleosides and 2'-deoxypurine nucleosides to the free base and ribose (or 2'-deoxyribose) 1-phosphate. Whereas the human enzyme is specific for 6-oxopurine ribonucleosides, the Escherichia coli enzyme accepts additional substrates including 6-oxopurine ribonucleosides, 6-aminopurine ribonucleosides, and to a lesser extent purine arabinosides. These differences have been exploited in a potential suicide gene therapy treatment for solid tumors. In an effort to optimize this suicide gene therapy approach, we have determined the three-dimensional structure of the E. coli enzyme in complex with 10 nucleoside analogs and correlated the structures with kinetic measurements and computer modeling. These studies explain the preference of the enzyme for ribose sugars, show increased flexibility for active site residues Asp204 and Arg24, and suggest that interactions involving the 1- and 6-positions of the purine and the 4'- and 5'-positions of the ribose provide the best opportunities to increase prodrug specificity and enzyme efficiency.
About this Structure
1PR2 is a Single protein structure of sequence from Escherichia coli, and escherichia coli o157:h7. Full crystallographic information is available from OCA.
Reference
Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase., Bennett EM, Li C, Allan PW, Parker WB, Ealick SE, J Biol Chem. 2003 Nov 21;278(47):47110-8. Epub 2003 Aug 21. PMID:12937174
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