1eyw: Difference between revisions

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[[Image:1eyw.gif|left|200px]]<br /><applet load="1eyw" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1eyw.gif|left|200px]]<br /><applet load="1eyw" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1eyw, resolution 1.90Å" />

'''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE'''<br />

==Overview==

Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the, detoxification of organophosphates such as the widely utilized insecticide, paraoxon and the chemical warfare agent sarin. The three-dimensional, structure of the enzyme is known from high resolution x-ray, crystallographic analyses. Each subunit of the homodimer folds into a, so-called TIM barrel, with eight strands of parallel beta-sheet. The two, zinc ions required for activity are positioned at the C-terminal portion, of the beta-barrel. Here, we describe the three-dimensional structure of, PTE complexed with the inhibitor diisopropyl methyl phosphonate, which, serves as a mimic for sarin. Additionally, the structure of the enzyme, complexed with triethyl phosphate is also presented. In the case of the, PTE-diisopropyl methyl phosphonate complex, the phosphoryl oxygen of the, inhibitor coordinates to the more solvent-exposed zinc ion (2.5 A), thereby lending support to the presumed catalytic mechanism involving, metal coordination of the substrate. In the PTE-triethyl phosphate, complex, the phosphoryl oxygen of the inhibitor is positioned at 3.4 A, from the more solvent-exposed zinc ion. The two structures described in, this report provide additional molecular understanding for the ability of, this remarkable enzyme to hydrolyze such a wide range of organophosphorus, substrates.

Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the detoxification of organophosphates such as the widely utilized insecticide paraoxon and the chemical warfare agent sarin. The three-dimensional structure of the enzyme is known from high resolution x-ray crystallographic analyses. Each subunit of the homodimer folds into a so-called TIM barrel, with eight strands of parallel beta-sheet. The two zinc ions required for activity are positioned at the C-terminal portion of the beta-barrel. Here, we describe the three-dimensional structure of PTE complexed with the inhibitor diisopropyl methyl phosphonate, which serves as a mimic for sarin. Additionally, the structure of the enzyme complexed with triethyl phosphate is also presented. In the case of the PTE-diisopropyl methyl phosphonate complex, the phosphoryl oxygen of the inhibitor coordinates to the more solvent-exposed zinc ion (2.5 A), thereby lending support to the presumed catalytic mechanism involving metal coordination of the substrate. In the PTE-triethyl phosphate complex, the phosphoryl oxygen of the inhibitor is positioned at 3.4 A from the more solvent-exposed zinc ion. The two structures described in this report provide additional molecular understanding for the ability of this remarkable enzyme to hydrolyze such a wide range of organophosphorus substrates.

==About this Structure==

1EYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta] with ZN, TEN and PEL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1EYW OCA].

1EYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=TEN:'>TEN</scene> and <scene name='pdbligand=PEL:'>PEL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYW OCA].

==Reference==

Line 14:

[[Category: Brevundimonas diminuta]]

[[Category: Single protein]]

[[Category: Benning, M.M.]]

[[Category: Benning, M M.]]

[[Category: Holden, H.M.]]

[[Category: Holden, H M.]]

[[Category: Hong, S.B.]]

[[Category: Hong, S B.]]

[[Category: Raushel, F.M.]]

[[Category: Raushel, F M.]]

[[Category: PEL]]

[[Category: TEN]]

Line 25:

[[Category: zinc]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 14~~:26:~~49 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1eyw.gif|left|200px]]<br /><applet load="1eyw" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1eyw.gif|left|200px]]<br /><applet load="1eyw" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1eyw, resolution 1.90&Aring;" />
 '''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE'''<br />
 ==Overview==
-Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the, detoxification of organophosphates such as the widely utilized insecticide, paraoxon and the chemical warfare agent sarin. The three-dimensional, structure of the enzyme is known from high resolution x-ray, crystallographic analyses. Each subunit of the homodimer folds into a, so-called TIM barrel, with eight strands of parallel beta-sheet. The two, zinc ions required for activity are positioned at the C-terminal portion, of the beta-barrel. Here, we describe the three-dimensional structure of, PTE complexed with the inhibitor diisopropyl methyl phosphonate, which, serves as a mimic for sarin. Additionally, the structure of the enzyme, complexed with triethyl phosphate is also presented. In the case of the, PTE-diisopropyl methyl phosphonate complex, the phosphoryl oxygen of the, inhibitor coordinates to the more solvent-exposed zinc ion (2.5 A), thereby lending support to the presumed catalytic mechanism involving, metal coordination of the substrate. In the PTE-triethyl phosphate, complex, the phosphoryl oxygen of the inhibitor is positioned at 3.4 A, from the more solvent-exposed zinc ion. The two structures described in, this report provide additional molecular understanding for the ability of, this remarkable enzyme to hydrolyze such a wide range of organophosphorus, substrates.
+Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the detoxification of organophosphates such as the widely utilized insecticide paraoxon and the chemical warfare agent sarin. The three-dimensional structure of the enzyme is known from high resolution x-ray crystallographic analyses. Each subunit of the homodimer folds into a so-called TIM barrel, with eight strands of parallel beta-sheet. The two zinc ions required for activity are positioned at the C-terminal portion of the beta-barrel. Here, we describe the three-dimensional structure of PTE complexed with the inhibitor diisopropyl methyl phosphonate, which serves as a mimic for sarin. Additionally, the structure of the enzyme complexed with triethyl phosphate is also presented. In the case of the PTE-diisopropyl methyl phosphonate complex, the phosphoryl oxygen of the inhibitor coordinates to the more solvent-exposed zinc ion (2.5 A), thereby lending support to the presumed catalytic mechanism involving metal coordination of the substrate. In the PTE-triethyl phosphate complex, the phosphoryl oxygen of the inhibitor is positioned at 3.4 A from the more solvent-exposed zinc ion. The two structures described in this report provide additional molecular understanding for the ability of this remarkable enzyme to hydrolyze such a wide range of organophosphorus substrates.
 ==About this Structure==
-EYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta] with ZN, TEN and PEL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EYW OCA].
+EYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=TEN:'>TEN</scene> and <scene name='pdbligand=PEL:'>PEL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYW OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Brevundimonas diminuta]]
 [[Category: Single protein]]
-[[Category: Benning, M.M.]]
+[[Category: Benning, M M.]]
-[[Category: Holden, H.M.]]
+[[Category: Holden, H M.]]
-[[Category: Hong, S.B.]]
+[[Category: Hong, S B.]]
-[[Category: Raushel, F.M.]]
+[[Category: Raushel, F M.]]
 [[Category: PEL]]
 [[Category: TEN]]
@@ Line 25: / Line 25: @@
 [[Category: zinc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:26:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:01 2008''