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| | <StructureSection load='5x6s' size='340' side='right'caption='[[5x6s]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5x6s' size='340' side='right'caption='[[5x6s]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x6s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspaw Aspaw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X6S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X6S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">axeA, aceA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=105351 ASPAW])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylxylan_esterase Acetylxylan esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.72 3.1.1.72] </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=5x6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6s OCA], [https://pdbe.org/5x6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x6s RCSB], [https://www.ebi.ac.uk/pdbsum/5x6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6s OCA], [http://pdbe.org/5x6s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x6s RCSB], [http://www.ebi.ac.uk/pdbsum/5x6s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AXE1_ASPAW AXE1_ASPAW] |
| | <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: Acetylxylan esterase]] | + | [[Category: Aspergillus awamori]] |
| - | [[Category: Aspaw]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Komiya, D]] | + | [[Category: Komiya D]] |
| - | [[Category: Koseki, T]] | + | [[Category: Koseki T]] |
| - | [[Category: Alpha/beta-hydrolase]]
| + | |
| - | [[Category: Cazy ce1]]
| + | |
| - | [[Category: Estrase_phb]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
AXE1_ASPAW
Publication Abstract from PubMed
Acetyl xylan esterase (AXE) catalyzes the hydrolysis of the acetyl bonds present in plant cell wall polysaccharides. Here, we determined the crystal structure of AXE from Aspergillus luchuensis (AlAXEA), providing the three-dimensional structure of an enzyme in the Esterase_phb family. AlAXEA shares its core alpha/beta-hydrolase fold structure with esterases in other families, but it has an extended central beta-sheet at both its ends and an extra loop. Structural comparison with a ferulic acid esterase (FAE) from Aspergillus niger indicated that AlAXEA has conserved catalytic machinery: a catalytic triad (Ser119, His259, and Asp202) and an oxyanion hole (Cys40 and Ser120). Near the catalytic triad of AlAXEA, two aromatic residues (Tyr39 and Trp160) form small pockets at both sides. Homology models of fungal FAEs in the same Esterase_phb family have wide pockets at the corresponding sites because they have residues with smaller side chains (Pro, Ser, and Gly). Site-directed mutants at Tyr39 showed similar substrate specificity to the wild-type enzyme, whereas those at Trp160 acquired an expanded substrate specificity. Interestingly, the Trp160 mutants acquired weak but significant type B-like FAE activity. Moreover, the engineered enzymes exhibited ferulic acid-releasing activity from wheat arabinoxylan.IMPORTANCE Hemicelluloses in the plant cell wall are often decorated by acetyl and ferulic acid groups. Therefore, complete and efficient degradation of plant polysaccharides requires the enzymes for cleaving the side chains of the polymer. Since the Esterase_phb family contains a wide array of fungal FAEs and AXEs from fungi and bacteria, our study will provide a structural basis for the molecular mechanism of these industrially relevant enzymes in biopolymer degradation. The structure of the Esterase_phb family also provides information for bacterial polyhydroxyalkanoate depolymerases that are involved in biodegradation of thermoplastic polymers.
Crystal Structure and Substrate Specificity Modification of Acetyl Xylan Esterase from Aspergillus luchuensis.,Komiya D, Hori A, Ishida T, Igarashi K, Samejima M, Koseki T, Fushinobu S Appl Environ Microbiol. 2017 Aug 11. pii: AEM.01251-17. doi:, 10.1128/AEM.01251-17. PMID:28802264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Komiya D, Hori A, Ishida T, Igarashi K, Samejima M, Koseki T, Fushinobu S. Crystal Structure and Substrate Specificity Modification of Acetyl Xylan Esterase from Aspergillus luchuensis. Appl Environ Microbiol. 2017 Aug 11. pii: AEM.01251-17. doi:, 10.1128/AEM.01251-17. PMID:28802264 doi:http://dx.doi.org/10.1128/AEM.01251-17
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