View source for 8yzo


==Crystal structural analysis of PaL mutant L297M==
<StructureSection load='8yzo' size='340' side='right'caption='[[8yzo]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8yzo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_alcaligenes Pseudomonas alcaligenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YZO 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]] 1.769&#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=8yzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yzo OCA], [https://pdbe.org/8yzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yzo RCSB], [https://www.ebi.ac.uk/pdbsum/8yzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yzo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H9MZI2_PSEAC H9MZI2_PSEAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Pseudomonas aeruginosa lipase PaL catalyzes the stereoselective hydrolysis of menthyl propionate to produce L-menthol. The lack of a three-dimensional structure of PaL has so far prevented a detailed understanding of its stereoselective reaction mechanism. Here, the crystal structure of PaL was determined at a resolution of 1.80 A by single-wavelength anomalous diffraction. In the apo-PaL structure, the catalytic His302 is located in a long loop on the surface that is solvent exposed. His302 is distant from the other two catalytic residues, Asp274 and Ser164. This configuration of catalytic residues is unusual for lipases. Using metadynamics simulations, we observed that the enzyme undergoes a significant conformational change upon ligand binding. We also explored the catalytic and stereoselectivity mechanisms of PaL by all-atom molecular dynamics simulations. These findings could guide the engineering of PaL with an improved diastereoselectivity for L-menthol production.

Crystal structure of lipase from Pseudomonas aeruginosa reveals an unusual catalytic triad conformation.,Xu G, Guo H, Yu Z, Wang S, Shen D, Yang L, Wu J, Chen B, Yu H Structure. 2024 Sep 5;32(9):1454-1464.e3. doi: 10.1016/j.str.2024.06.014. Epub , 2024 Jul 17. PMID:39025068<ref>PMID:39025068</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8yzo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas alcaligenes]]
[[Category: Wu J]]
[[Category: Xu G]]