5a6v: Difference between revisions
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==Open and closed conformations and protonation states of Candida antarctica Lipase B: Xenon complex== | |||
<StructureSection load='5a6v' size='340' side='right'caption='[[5a6v]], [[Resolution|resolution]] 2.28Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a6v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moesziomyces_antarcticus Moesziomyces antarcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A6V 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]] 2.28Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XE:XENON'>XE</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=5a6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a6v OCA], [https://pdbe.org/5a6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a6v RCSB], [https://www.ebi.ac.uk/pdbsum/5a6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a6v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LIPB_PSEA2 LIPB_PSEA2] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lipases (E.C. 3.1.1.3) are ubiquitous hydrolases for the carboxyl ester bond of water-insoluble substrates such as triacylglycerols, phospholipids, and other insoluble substrates, acting in aqueous as well as in low-water media, thus being of considerable physiological significance with high interest also for their industrial applications. The hydrolysis reaction follows a two-step mechanism, or 'interfacial activation', with adsorption of the enzyme to an heterogeneous interface and subsequent enhancement of the lipolytic activity. Among lipases, Candida antarctica Lipase B (CALB) has never shown any significant interfacial activation, and a closed conformation of CALB has never been reported leading to the conclusion that its behaviour was due to the absence of a lid regulating the access to the active site. The lid open and closed conformations and their protonation states are observed in the crystal structure of CALB at 0.91 A resolution. Having the open and closed states at atomic resolution allows relating protonation to the conformation, indicating the role of Asp145 and Lys290 in the conformation alteration. The findings explain the lack of 'interfacial activation' of CALB and offer new elements to elucidate this mechanism, with the consequent implications for the catalytic properties and classification of lipases. | |||
Open and closed states of Candida antarctica Lipase B: protonation and the mechanism of interfacial activation.,Stauch B, Fisher SJ, Cianci M J Lipid Res. 2015 Oct 7. pii: jlr.M063388. PMID:26447231<ref>PMID:26447231</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5a6v" style="background-color:#fffaf0;"></div> | ||
[[Category: Cianci | |||
[[Category: Stauch | ==See Also== | ||
*[[Lipase 3D Structures|Lipase 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Moesziomyces antarcticus]] | |||
[[Category: Cianci M]] | |||
[[Category: Fisher SJ]] | |||
[[Category: Stauch B]] | |||
Latest revision as of 14:04, 10 January 2024
Open and closed conformations and protonation states of Candida antarctica Lipase B: Xenon complexOpen and closed conformations and protonation states of Candida antarctica Lipase B: Xenon complex
Structural highlights
FunctionLIPB_PSEA2 Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. Publication Abstract from PubMedLipases (E.C. 3.1.1.3) are ubiquitous hydrolases for the carboxyl ester bond of water-insoluble substrates such as triacylglycerols, phospholipids, and other insoluble substrates, acting in aqueous as well as in low-water media, thus being of considerable physiological significance with high interest also for their industrial applications. The hydrolysis reaction follows a two-step mechanism, or 'interfacial activation', with adsorption of the enzyme to an heterogeneous interface and subsequent enhancement of the lipolytic activity. Among lipases, Candida antarctica Lipase B (CALB) has never shown any significant interfacial activation, and a closed conformation of CALB has never been reported leading to the conclusion that its behaviour was due to the absence of a lid regulating the access to the active site. The lid open and closed conformations and their protonation states are observed in the crystal structure of CALB at 0.91 A resolution. Having the open and closed states at atomic resolution allows relating protonation to the conformation, indicating the role of Asp145 and Lys290 in the conformation alteration. The findings explain the lack of 'interfacial activation' of CALB and offer new elements to elucidate this mechanism, with the consequent implications for the catalytic properties and classification of lipases. Open and closed states of Candida antarctica Lipase B: protonation and the mechanism of interfacial activation.,Stauch B, Fisher SJ, Cianci M J Lipid Res. 2015 Oct 7. pii: jlr.M063388. PMID:26447231[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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