4gw3: Difference between revisions
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==Crystal Structure of the Lipase from Proteus mirabilis== | ==Crystal Structure of the Lipase from Proteus mirabilis== | ||
<StructureSection load='4gw3' size='340' side='right' caption='[[4gw3]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4gw3' size='340' side='right'caption='[[4gw3]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gw3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4gw3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GW3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=4gw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gw3 OCA], [https://pdbe.org/4gw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gw3 RCSB], [https://www.ebi.ac.uk/pdbsum/4gw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gw3 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B4EVM3_PROMH B4EVM3_PROMH] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Proteus mirabilis]] | ||
[[Category: Korman | [[Category: Korman TP]] | ||
Revision as of 10:22, 26 October 2022
Crystal Structure of the Lipase from Proteus mirabilisCrystal Structure of the Lipase from Proteus mirabilis
Structural highlights
FunctionPublication Abstract from PubMedBacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45 degrees C and are used extensively as biocatalysts. The lipase from Proteus mirabilis belongs to the Proteus/psychrophilic subfamily of lipase family I.1 and is a promising catalyst for biodiesel production because it can tolerate high amounts of water in the reaction. Here we present the crystal structure of the Proteus mirabilis lipase, a member of the Proteus/psychrophilic subfamily of I.1lipases. The structure of the Proteus mirabilis lipase was solved in the absence and presence of a bound phosphonate inhibitor. Unexpectedly, both the apo and inhibitor bound forms of P. mirabilis lipase were found to be in a closed conformation. The structure reveals a unique oxyanion hole and a wide active site that is solvent accessible even in the closed conformation. A distinct mechanism for Ca(2+) coordination may explain how these lipases can fold without specific chaperones. Crystal Structure of Proteus mirabilis Lipase, a Novel Lipase from the Proteus/Psychrophilic Subfamily of Lipase Family I.1.,Korman TP, Bowie JU PLoS One. 2012;7(12):e52890. doi: 10.1371/journal.pone.0052890. Epub 2012 Dec 26. PMID:23300806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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