|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal structure of Fusarium oxysporum cutinase== | | ==Crystal structure of Fusarium oxysporum cutinase== |
| - | <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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AJH FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </span></td></tr> | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ajh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ajh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ajh RCSB], [http://www.ebi.ac.uk/pdbsum/5ajh PDBsum]</span></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=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 == |
| - | [[http://www.uniprot.org/uniprot/X0BTD8_FUSOX X0BTD8_FUSOX]] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle.[RuleBase:RU361263] | + | [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 == |
| Line 17: |
Line 18: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 5ajh" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cutinase 3D structures|Cutinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cutinase]] | + | [[Category: Fusarium oxysporum f. sp. raphani 54005]] |
| - | [[Category: Christakopoulos, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Dimarogona, M]] | + | [[Category: Christakopoulos P]] |
| - | [[Category: Kanelli, M]] | + | [[Category: Dimarogona M]] |
| - | [[Category: Nikolaivits, E]] | + | [[Category: Kanelli M]] |
| - | [[Category: Sandgren, M]] | + | [[Category: Nikolaivits E]] |
| - | [[Category: Topakas, E]] | + | [[Category: Sandgren M]] |
| - | [[Category: Alpha/beta hydrolase fold]]
| + | [[Category: Topakas E]] |
| - | [[Category: Esterase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pet modification]]
| + | |
| Structural highlights
Function
X0BTD8_FUSOX Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle.[RuleBase:RU361263]
Publication Abstract from PubMed
BACKGROUND: 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 Also
References
- ↑ Dimarogona M, Nikolaivits E, Kanelli M, Christakopoulos P, Sandgren M, Topakas E. Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential. Biochim Biophys Acta. 2015 Aug 17. pii: S0304-4165(15)00218-4. doi:, 10.1016/j.bbagen.2015.08.009. PMID:26291558 doi:http://dx.doi.org/10.1016/j.bbagen.2015.08.009
|
