2o1c: Difference between revisions

Revision as of 09:47, 18 February 2009

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File:2o1c.png

Template:STRUCTURE 2o1c

Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolaseStructure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase

About this StructureAbout this Structure

2O1C is a 4 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}^{[xtra 2]}

↑ O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J Biol Chem. 1996 Oct 4;271(40):24649-54. PMID:8798731
↑ Suzuki Y, Brown GM. The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J Biol Chem. 1974 Apr 25;249(8):2405-10. PMID:4362677

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[1] O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J Biol Chem. 1996 Oct 4;271(40):24649-54. PMID:8798731

[2] Suzuki Y, Brown GM. The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J Biol Chem. 1974 Apr 25;249(8):2405-10. PMID:4362677

[xtra 1]

[xtra 2]

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-[[Image:2o1c.jpg|left|200px]]
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 {{STRUCTURE_2o1c|  PDB=2o1c  |  SCENE=  }}
-'''Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase'''
+===Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase===
-==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==
-O1C 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=2O1C OCA].
+O1C is a 4 chains structure of sequences 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=2O1C 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:[http://www.ncbi.nlm.nih.gov/pubmed/8798731 8798731]
+<ref group="xtra">PMID:8798731</ref><ref group="xtra">PMID:4362677</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
 [[Category: Amzel, L M.]]
 [[Category: Bianchet, M A.]]
 [[Category: Gabelli, S B.]]
 [[Category: Nudix ntp hydrolase ntp pyrophosphohydrolase mutt dihydroneopterin triphosphate pyrophosphohydrolase folate biosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:11:14 2008''
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