View source for 3wmt


==Crystal structure of feruloyl esterase B from Aspergillus oryzae==
<StructureSection load='3wmt' size='340' side='right'caption='[[3wmt]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wmt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae_RIB40 Aspergillus oryzae RIB40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WMT 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3wmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmt OCA], [https://pdbe.org/3wmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wmt RCSB], [https://www.ebi.ac.uk/pdbsum/3wmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FAEB1_ASPOR FAEB1_ASPOR] Involved in degradation of plant cell walls. Hydrolyzes of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin (By similarity).
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== Publication Abstract from PubMed ==
Feruloyl esterase (FAE) catalyzes the hydrolysis of the ferulic and diferulic acids present in plant cell wall polysaccharides, and tannase catalyzes the hydrolysis of tannins to release gallic acid. The fungal tannase family in the ESTHER database contains various enzymes, including FAEs and tannases. Despite the importance of FAEs and tannases in bioindustrial applications, three-dimensional structures of the fungal tannase family members have been unknown. Here, we determined the crystal structure of FAE B from Aspergillus oryzae (AoFaeB), which belongs to the fungal tannase family, at 1.5 A resolution. AoFaeB consists of a catalytic alpha/beta-hydrolase fold domain and a large lid domain, and the latter has a novel fold. To estimate probable binding models of substrates in AoFaeB, an automated docking analysis was performed. In the active site pocket of AoFaeB, residues responsible for the substrate specificity of the FAE activity were identified. The catalytic triad of AoFaeB comprises Ser203, Asp417, and His457, and the serine and histidine residues are directly connected by a disulfide bond of the neighboring cysteine residues, Cys202 and Cys458. This structural feature, the "CS-D-HC motif," is unprecedented in serine hydrolases. A mutational analysis indicated that the novel structural motif plays essential roles in the function of the active site.

Crystal structure of a feruloyl esterase belonging to the tannase family: a disulfide bond near a catalytic triad.,Suzuki K, Hori A, Kawamoto K, Thangudu RR, Ishida T, Igarashi K, Samejima M, Yamada C, Arakawa T, Wakagi T, Koseki T, Fushinobu S Proteins. 2014 Oct;82(10):2857-67. doi: 10.1002/prot.24649. Epub 2014 Aug 11. PMID:25066066<ref>PMID:25066066</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3wmt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Aspergillus oryzae RIB40]]
[[Category: Large Structures]]
[[Category: Fushinobu S]]
[[Category: Igarashi K]]
[[Category: Ishida T]]
[[Category: Koseki T]]
[[Category: Suzuki K]]