6fat

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==The crystal structure of a feruloyl esterase C from Fusarium oxysporum.==
==The crystal structure of a feruloyl esterase C from Fusarium oxysporum.==
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<StructureSection load='6fat' size='340' side='right' caption='[[6fat]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='6fat' size='340' side='right'caption='[[6fat]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6fat]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FAT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6fat]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FAT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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=6fat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fat OCA], [http://pdbe.org/6fat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fat RCSB], [http://www.ebi.ac.uk/pdbsum/6fat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fat ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fat OCA], [https://pdbe.org/6fat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fat RCSB], [https://www.ebi.ac.uk/pdbsum/6fat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fat ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1D3S5H0_FUSOX A0A1D3S5H0_FUSOX]
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A hypothetical protein FoFaeC-12213 of Fusarium oxysporum was found to have high amino acid sequence identity with known type C feruloyl esterases (FAEs) containing a 13-amino acid conserved region flanking the characteristic G-X-S-X-G motif of a serine esterase. The putative FAE from the genomic DNA was successfully cloned in frame with the Saccharomyces cerevisiae alpha-factor secretion signal under the transcriptional control of the alcohol oxidase (AOX1) promoter and integrated in Pichia pastoris X-33 to confirm that the enzyme exhibits FAE activity. The molecular weight (62 kDa) and pI (6.8) were in agreement with the theoretical calculated values indicating the correct processing of the secretion signal in P. pastoris. The recombinant FAE was purified to its homogeneity and subsequently characterized using a series of model substrates including methyl esters of hydroxycinnamates, alkyl ferulates and monoferuloylated 4-nitrophenyl glycosides. The substrate specificity profiling reveals that the enzyme is a type C FAE showing broad hydrolytic activity against the four methyl esters of hydroxycinnamic acids and strong preference for the hydrolysis of n-propyl ferulate. Ferulic acid (FA) was efficiently released from destarched wheat bran when the esterase was incubated together with xylanase from Trichoderma longibrachiatum (a maximum of 67% total FA released after 1-h incubation). The esterase showed broad pH stability making it an important candidate for alkaline applications such as pulp treatment in the paper industry.
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Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum.,Moukouli M, Topakas E, Christakopoulos P Appl Microbiol Biotechnol. 2008 May;79(2):245-54. doi: 10.1007/s00253-008-1432-3. PMID:18414848<ref>PMID:18414848</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6fat" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chrysina, E D]]
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[[Category: Fusarium oxysporum]]
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[[Category: Dimarogona, M]]
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[[Category: Large Structures]]
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[[Category: Ferulic acid esterase]]
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[[Category: Chrysina ED]]
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[[Category: Hydrolase]]
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[[Category: Dimarogona M]]

Current revision

The crystal structure of a feruloyl esterase C from Fusarium oxysporum.

PDB ID 6fat

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