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[[Image:1bf6.jpg|left|200px]]


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==PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI==
The line below this paragraph, containing "STRUCTURE_1bf6", creates the "Structure Box" on the page.
<StructureSection load='1bf6' size='340' side='right'caption='[[1bf6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1bf6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BF6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_1bf6|  PDB=1bf6  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf6 OCA], [https://pdbe.org/1bf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bf6 ProSAT]</span></td></tr>
 
</table>
'''PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI'''
== Function ==
 
[https://www.uniprot.org/uniprot/PHP_ECOLI PHP_ECOLI] Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: P-nitrophenyl acetate, L-alanine nitroanilide, P-nitrophenyl sulfate, bis(P-nitrophenyl) phosphate, paraoxon, and P-nitrophenyl phosphate. No enzymatic activity was detected with any of these nonspecific substrates.
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bf6_consurf.spt"</scriptWhenChecked>
1BF6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF6 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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:[http://www.ncbi.nlm.nih.gov/pubmed/9548740 9548740]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bf6 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Buchbinder, J L.]]
[[Category: Buchbinder JL]]
[[Category: Fletterick, R J.]]
[[Category: Fletterick RJ]]
[[Category: Scanlan, T S.]]
[[Category: Scanlan TS]]
[[Category: Stephenson, R C.]]
[[Category: Stephenson RC]]
[[Category: Hypothetical protein]]
[[Category: Phosphotriesterase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:26:11 2008''

Latest revision as of 09:35, 7 February 2024

PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLIPHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI

Structural highlights

1bf6 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHP_ECOLI Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: P-nitrophenyl acetate, L-alanine nitroanilide, P-nitrophenyl sulfate, bis(P-nitrophenyl) phosphate, paraoxon, and P-nitrophenyl phosphate. No enzymatic activity was detected with any of these nonspecific substrates.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1bf6, resolution 1.70Å

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