View source for 5ioj


==Crystal structure of the Sphingobium sp. TCM1 phosphotriesterase without the binuclear manganese center==
<StructureSection load='5ioj' size='340' side='right'caption='[[5ioj]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ioj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_sp._TCM1 Sphingobium sp. TCM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IOJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ioj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ioj OCA], [https://pdbe.org/5ioj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ioj RCSB], [https://www.ebi.ac.uk/pdbsum/5ioj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ioj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A077JBW9_9SPHN A0A077JBW9_9SPHN] 
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== Publication Abstract from PubMed ==
A novel phosphotriesterase was recently discovered and purified from Sphingobium sp. TCM1 (Sb-PTE) and shown to catalyze the hydrolysis of a broad spectrum of organophosphate esters with a catalytic efficiency that exceeds 106 M-1 s-1 for the hydrolysis of triphenyl phosphate. The enzyme was crystallized and the three-dimensional structure determined to a resolution of 2.1 A using single-wavelength anomalous diffraction (Protein Data Bank entry 5HRM ). The enzyme adopts a seven-bladed beta-propeller protein fold, and three disulfide bonds were identified between Cys-146 and Cys-242, Cys-411 and Cys-443, and Cys-542 and Cys-559. The active site of Sb-PTE contains a binuclear manganese center that is nearly identical to that of the structurally unrelated phosphotriesterase from Pseudomonas diminuta (Pd-PTE). The two metal ions in the active site are bridged to one another by Glu-201 and a water molecule. The alpha-metal ion is further coordinated to the protein by interactions with His-389, His-475, and Glu-407, whereas the beta-metal ion is further liganded to His-317 and His-258. Computational docking of mimics of the proposed pentavalent reaction intermediates for the hydrolysis of organophosphates was used to provide a model for the binding of chiral substrates in the active site of Sb-PTE. The most striking difference in the catalytic properties of Sb-PTE, relative to those of Pd-PTE, is the enhanced rate of hydrolysis of organophosphate esters with substantially weaker leaving groups. The structural basis for this difference in the catalytic properties between Sb-PTE and Pd-PTE, despite the nearly identical binuclear metal centers for the activation of the substrate and nucleophilic water molecule, is at present unclear.

Structure of a Novel Phosphotriesterase from Sphingobium sp. TCM1: A Familiar Binuclear Metal Center Embedded in a Seven-Bladed beta-Propeller Protein Fold.,Mabanglo MF, Xiang DF, Bigley AN, Raushel FM Biochemistry. 2016 Jul 8. PMID:27353520<ref>PMID:27353520</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ioj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sphingobium sp. TCM1]]
[[Category: Mabanglo MF]]
[[Category: Raushel FM]]