2o5w
From Proteopedia
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| - | [[Image:2o5w.jpg|left|200px]] | + | [[Image:2o5w.jpg|left|200px]] |
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| - | '''Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase in complex with Sm+3 and pyrophosphate''' | + | {{Structure |
| + | |PDB= 2o5w |SIZE=350|CAPTION= <scene name='initialview01'>2o5w</scene>, resolution 2.600Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= nudB, ntpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase in complex with Sm+3 and pyrophosphate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O5W is a [ | + | 2O5W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O5W OCA]. |
==Reference== | ==Reference== | ||
| - | Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme., O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ, J Biol Chem. 1996 Oct 4;271(40):24649-54. PMID:[http:// | + | Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme., O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ, J Biol Chem. 1996 Oct 4;271(40):24649-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8798731 8798731] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dihydroneopterin triphosphate pyrophosphohydrolase nudix nucleoside triphosphate pyrophosphohydrolase mutt]] | [[Category: dihydroneopterin triphosphate pyrophosphohydrolase nudix nucleoside triphosphate pyrophosphohydrolase mutt]] | ||
| - | ''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 17:55:31 2008'' |
Revision as of 15:55, 20 March 2008
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| , resolution 2.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | nudB, ntpA (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase in complex with Sm+3 and pyrophosphate
Overview
The product of the Escherichia coli orf17 gene is a novel nucleoside triphosphate pyrophosphohydrolase with a preference for dATP over the other canonical (deoxy)nucleoside triphosphates, and it catalyzes the hydrolysis of dATP through a nucleophilic attack at the beta-phosphorus to produce dAMP and inorganic pyrophosphate. It has a pH optimum between 8.5 and 9.0, a divalent metal ion requirement with optimal activity at 5 mM Mg2+, a Km of 0.8 mM and a kcat of 5.2 s-1 at 37 degrees C for dATP. dAMP is a weak competitive inhibitor with a Ki of approximately 4 mM, while PPi is a much stronger inhibitor with an apparent Ki of approximately 20 microM. The enzyme contains the highly conserved signature sequence GXVEX2ETX6REVXEEX2I designating the MutT family of proteins. However, unlike the other nucleoside triphosphate pyrophosphohydrolases with this conserved sequence, the Orf17 protein does not complement the mutT- mutator phenotype, and thus must serve a different biological role in the cell.
About this Structure
2O5W is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme., O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ, J Biol Chem. 1996 Oct 4;271(40):24649-54. PMID:8798731
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