1bf6: Difference between revisions
New page: left|200px<br /><applet load="1bf6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bf6, resolution 1.7Å" /> '''PHOSPHOTRIESTERASE HO... |
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[[Image:1bf6.jpg|left|200px]]<br /><applet load="1bf6" size=" | [[Image:1bf6.jpg|left|200px]]<br /><applet load="1bf6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bf6, resolution 1.7Å" /> | caption="1bf6, resolution 1.7Å" /> | ||
'''PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI'''<br /> | '''PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
Phosphotriesterase homology protein (PHP) is a member of a recently | Phosphotriesterase homology protein (PHP) is a member of a recently discovered family of proteins related to phosphotriesterase, a hydrolytic, bacterial enzyme with an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates, which are common constituents of chemical warfare agents and agricultural pesticides. No natural substrate has been identified for phosphotriesterase, and it has been suggested that the enzyme may have evolved the ability to hydrolyze synthetic compounds in bacteria under selective pressure to meet nutritional needs. PHP, which has 28% sequence identity with phosphotriesterase, may belong to the family of proteins from which phosphotriesterase evolved. Here we report the cloning, expression, initial characterization, and high-resolution X-ray crystallographic structure of PHP. Biochemical analysis shows that PHP is monomeric and binds two zinc ions per monomer. Unlike phosphotriesterase, PHP does not catalyze the hydrolysis of nonspecific phosphotriesters. The structure, similar to that of phosphotriesterase, consists of a long, elliptical alpha/beta barrel and has a binuclear zinc center in a cleft at the carboxy end of the barrel at the location of the presumptive active site. | ||
==About this Structure== | ==About this Structure== | ||
1BF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, SO4, MPD and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1BF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MPD:'>MPD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Buchbinder, J | [[Category: Buchbinder, J L.]] | ||
[[Category: Fletterick, R | [[Category: Fletterick, R J.]] | ||
[[Category: Scanlan, T | [[Category: Scanlan, T S.]] | ||
[[Category: Stephenson, R | [[Category: Stephenson, R C.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
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[[Category: phosphotriesterase]] | [[Category: phosphotriesterase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:37 2008'' | ||
Revision as of 12:54, 21 February 2008
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PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI
OverviewOverview
Phosphotriesterase homology protein (PHP) is a member of a recently discovered family of proteins related to phosphotriesterase, a hydrolytic, bacterial enzyme with an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates, which are common constituents of chemical warfare agents and agricultural pesticides. No natural substrate has been identified for phosphotriesterase, and it has been suggested that the enzyme may have evolved the ability to hydrolyze synthetic compounds in bacteria under selective pressure to meet nutritional needs. PHP, which has 28% sequence identity with phosphotriesterase, may belong to the family of proteins from which phosphotriesterase evolved. Here we report the cloning, expression, initial characterization, and high-resolution X-ray crystallographic structure of PHP. Biochemical analysis shows that PHP is monomeric and binds two zinc ions per monomer. Unlike phosphotriesterase, PHP does not catalyze the hydrolysis of nonspecific phosphotriesters. The structure, similar to that of phosphotriesterase, consists of a long, elliptical alpha/beta barrel and has a binuclear zinc center in a cleft at the carboxy end of the barrel at the location of the presumptive active site.
About this StructureAbout this Structure
1BF6 is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family., Buchbinder JL, Stephenson RC, Dresser MJ, Pitera JW, Scanlan TS, Fletterick RJ, Biochemistry. 1998 Apr 14;37(15):5096-106. PMID:9548740
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