3upm: Difference between revisions
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New page: '''Unreleased structure''' The entry 3upm is ON HOLD Authors: Tsai, P., Fox, N.G., Li, Y., Barondeau, D.P., Raushel, F.M. Description: Crystal Structure of PTE mutant H254Q/H257F/K185R... |
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The | ==Crystal Structure of PTE mutant H254Q/H257F/K185R/I274N== | ||
<StructureSection load='3upm' size='340' side='right'caption='[[3upm]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3upm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UPM 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]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</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=3upm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3upm OCA], [https://pdbe.org/3upm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3upm RCSB], [https://www.ebi.ac.uk/pdbsum/3upm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3upm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OPD_BREDI OPD_BREDI] Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate. | |||
==See Also== | |||
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brevundimonas diminuta]] | |||
[[Category: Large Structures]] | |||
[[Category: Barondeau DP]] | |||
[[Category: Fox NG]] | |||
[[Category: Li Y]] | |||
[[Category: Raushel FM]] | |||
[[Category: Tsai P]] | |||
Latest revision as of 17:05, 14 March 2024
Crystal Structure of PTE mutant H254Q/H257F/K185R/I274NCrystal Structure of PTE mutant H254Q/H257F/K185R/I274N
Structural highlights
FunctionOPD_BREDI Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate. See Also |
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