This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1eyw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eyw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1eyw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eyw| PDB=1eyw | SCENE= }}
{{STRUCTURE_1eyw| PDB=1eyw | SCENE= }}
-
'''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE'''
+
===THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10871616}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10871616 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10871616}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Organophosphate]]
[[Category: Organophosphate]]
[[Category: Zinc]]
[[Category: Zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:41:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:14:00 2008''

Revision as of 23:14, 30 June 2008

Image:1eyw.png

Template:STRUCTURE 1eyw

THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE

Template:ABSTRACT PUBMED 10871616

About this Structure

1EYW is a Single protein structure of sequence from Brevundimonas diminuta. Full crystallographic information is available from OCA.

Reference

The binding of substrate analogs to phosphotriesterase., Benning MM, Hong SB, Raushel FM, Holden HM, J Biol Chem. 2000 Sep 29;275(39):30556-60. PMID:10871616

Page seeded by OCA on Tue Jul 1 02:14:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eyw"
Personal tools