View source for 7bfu


==Thermogutta terrifontis esterase 2 phosphonylated by sarin==
<StructureSection load='7bfu' size='340' side='right'caption='[[7bfu]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermogutta_terrifontis Thermogutta terrifontis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BFU 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=SGB:O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE'>SGB</scene></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=7bfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bfu OCA], [https://pdbe.org/7bfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bfu RCSB], [https://www.ebi.ac.uk/pdbsum/7bfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bfu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A286RIX1_9BACT A0A286RIX1_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Organophosphorous nerve agents (OPNA) pose an actual and major threat for both military and civilians alike, as an upsurge in their use has been observed in the recent years. Currently available treatments mitigate the effect of the nerve agents, and could be vastly improved by means of scavengers of the nerve agents. Consequently, efforts have been made over the years into investigating enzymes, also known as bioscavengers, which have the potential either to trap or hydrolyze these toxic compounds. We investigated the previously described esterase 2 from Thermogutta terrifontis (TtEst2) as a potential bioscavenger of nerve agents. As such, we assessed its potential against G-agents (tabun, sarin, and cyclosarin), VX, as well as the pesticide paraoxon. We report that TtEst2 is a good bioscavenger of paraoxon and G-agents, but is rather slow at scavenging VX. X-ray crystallography studies showed that TtEst2 forms an irreversible complex with the aforementioned agents, and allowed the identification of amino-acids, whose mutagenesis could lead to better scavenging properties for VX. In conjunction with its cheap production and purification processes, as well as a robust structural backbone, further engineering of TtEst2 could lead to a stopgap bioscavenger useful for in corpo scavenging or skin decontamination.

A Thermophilic Bacterial Esterase for Scavenging Nerve Agents: A Kinetic, Biophysical and Structural Study.,Bzdrenga J, Trenet E, Chantegreil F, Bernal K, Nachon F, Brazzolotto X Molecules. 2021 Jan 27;26(3). pii: molecules26030657. doi:, 10.3390/molecules26030657. PMID:33513869<ref>PMID:33513869</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bfu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermogutta terrifontis]]
[[Category: Brazzolotto XB]]
[[Category: Bzdrenga J]]
[[Category: Nachon F]]