1psc: Difference between revisions

Revision as of 13:57, 27 July 2008

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File:1psc.png

Template:STRUCTURE 1psc

PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTAPHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA

Template:ABSTRACT PUBMED 7794910

About this StructureAbout this Structure

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

ReferenceReference

Three-dimensional structure of the binuclear metal center of phosphotriesterase., Benning MM, Kuo JM, Raushel FM, Holden HM, Biochemistry. 1995 Jun 27;34(25):7973-8. PMID:7794910

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OCA

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 {{STRUCTURE_1psc|  PDB=1psc  |  SCENE=  }}
-'''PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA'''
+===PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA===
-==Overview==
+<!--
-Phosphotriesterase, as isolated from Pseudomonas diminuta, is capable of detoxifying widely used pesticides such as paraoxon and parathion and various mammalian acetylcholinesterase inhibitors. The enzyme requires a binuclear metal center for activity. Recently, the three-dimensional structure of the apoenzyme was solved (Benning et al., 1994) and shown to consist of an alpha/beta-barrel. Here we describe the three-dimensional structure of the holoenzyme, reconstituted with cadmium, as determined by X-ray crystallographic analysis to 2.0-A resolution. Crystals employed in the investigation belonged to the space group C2 with unit cell dimensions of a = 129.5 A, b = 91.4 A, c = 69.4 A, beta = 91.9 degrees, and two subunits in the asymmetric unit. There are significant differences in the three-dimensional architecture of the apo and holo forms of the enzyme such that their alpha-carbon positions superimpose with a root-mean-square deviation of 3.4 A. The binuclear metal center is located at the C-terminus of the beta-barrel with the cadmiums separated by 3.8 A. There are two bridging ligands to the metals: a water molecule (or possibly a hydroxide ion) and a carbamylated lysine residue (Lys 169). The more buried cadmium is surrounded by His 55, His 57, Lys 169, Asp 301, and the bridging water in a trigonal bipyramidal arrangement. The second metal is coordinated in a distorted octahedral geometry by His 201, His 230, Lys 169, the bridging water molecule, and two additional solvents.
+The line below this paragraph, {{ABSTRACT_PUBMED_7794910}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7794910 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7794910}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Phosphoric triester]]
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