1pta: Difference between revisions

Revision as of 03:57, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pta.png

Template:STRUCTURE 1pta

THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTSTHREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS

Template:ABSTRACT PUBMED 7999757

About this StructureAbout this Structure

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

ReferenceReference

Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents., Benning MM, Kuo JM, Raushel FM, Holden HM, Biochemistry. 1994 Dec 20;33(50):15001-7. PMID:7999757

Page seeded by OCA on Mon Jul 28 03:57:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1pta.jpg|left|200px]]
+{{Seed}}
+[[Image:1pta.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1pta|  PDB=1pta  |  SCENE=  }}
-'''THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS'''
+===THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS===
-==Overview==
+<!--
-Organophosphates, such as parathion and paraoxon, constitute the largest class of insecticides currently used in industrialized nations. In addition, many of these compounds are known to inhibit mammalian acetylcholinesterases thereby acting as nerve agents. Consequently, organophosphate-degrading enzymes are of considerable interest in light of their ability to detoxify such compounds. Here we report the three-dimensional structure of such an enzyme, namely, phosphotriesterase, as determined by single crystal X-ray diffraction analysis to 2.1-A resolution. Crystals employed in this investigation belonged to the space group P2(1)2(1)2 with unit cell dimensions of a = 80.3 A, b = 93.4 A, and c = 44.8 A and one molecule per asymmetric unit. The structure was solved by multiple isomorphous replacement with two heavy-atom derivatives and refined to a crystallographic R factor of 18.0%. As observed in various other enzymes, the overall fold of the molecule consists of an alpha/beta barrel with eight strands of parallel beta-pleated sheet. In addition, there are two antiparallel beta-strands at the N-terminus. The molecular model of phosphotriesterase presented here provides the initial structural framework necessary toward understanding the enzyme's broad substrate specificities and its catalytic mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_7999757}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7999757 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7999757}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Benning, M.]]
 [[Category: Holden, H M.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:27:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:57:28 2008''