5ajh: Difference between revisions
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<StructureSection load='5ajh' size='340' side='right'caption='[[5ajh]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5ajh' size='340' side='right'caption='[[5ajh]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ajh]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ajh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum_f._sp._raphani_54005 Fusarium oxysporum f. sp. raphani 54005]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AJH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ajh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ajh OCA], [https://pdbe.org/5ajh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ajh RCSB], [https://www.ebi.ac.uk/pdbsum/5ajh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ajh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/X0BTD8_FUSOX X0BTD8_FUSOX] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle.[RuleBase:RU361263] | ||
<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: Fusarium oxysporum f. sp. raphani 54005]] | [[Category: Fusarium oxysporum f. sp. raphani 54005]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Christakopoulos | [[Category: Christakopoulos P]] | ||
[[Category: Dimarogona | [[Category: Dimarogona M]] | ||
[[Category: Kanelli | [[Category: Kanelli M]] | ||
[[Category: Nikolaivits | [[Category: Nikolaivits E]] | ||
[[Category: Sandgren | [[Category: Sandgren M]] | ||
[[Category: Topakas | [[Category: Topakas E]] | ||
Latest revision as of 14:10, 10 January 2024
Crystal structure of Fusarium oxysporum cutinaseCrystal structure of Fusarium oxysporum cutinase
Structural highlights
FunctionX0BTD8_FUSOX Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle.[RuleBase:RU361263] Publication Abstract from PubMedBACKGROUND: Cutinases are serine hydrolases that degrade cutin, a polyester of fatty acids that is the main component of plant cuticle. These biocatalysts have recently attracted increased biotechnological interest due to their potential to modify and degrade polyethylene terephthalate (PET), as well as other synthetic polymers. METHODS: A cutinase from the mesophilic fungus Fusarium oxysporum, named FoCut5a, was expressed either in the cytoplasm or periplasm of Escherichia coli BL21. Its X-ray structure was determined to 1.9A resolution using molecular replacement. The activity of the recombinant enzyme was tested on a variety of synthetic esters and polyester analogues. RESULTS: The highest production of recombinant FoCut5a was achieved using periplasmic expression at 16 degrees C. Its crystal structure is highly similar to previously determined Fusarium solani cutinase structure. However, a more detailed comparison of the surface properties and amino acid interactions revealed differences with potential impact on the biochemical properties of the two enzymes. FoCut5a showed maximum activity at 40 degrees C and pH8.0, while it was active on three p-nitrophenyl synthetic esters of aliphatic acids (C2, C4, C12), with the highest catalytic efficiency for the hydrolysis of the butyl ester. The recombinant cutinase was also found capable of hydrolyzing PET model substrates and synthetic polymers. CONCLUSIONS: The first reported expression and crystal structure determination of a functional cutinase from the mesophilic fungus F. oxysporum with potential application in surface modification of PET synthetic polymers. GENERAL SIGNIFICANCE: FoCut5a could be used as a biocatalyst in industrial applications for the environmentally-friendly treatment of synthetic polymers. Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential.,Dimarogona M, Nikolaivits E, Kanelli M, Christakopoulos P, Sandgren M, Topakas E Biochim Biophys Acta. 2015 Aug 17. pii: S0304-4165(15)00218-4. doi:, 10.1016/j.bbagen.2015.08.009. PMID:26291558[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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