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- | {{Seed}} | |
- | [[Image:1uwc.png|left|200px]] | |
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- | <!-- | + | ==Feruloyl esterase from Aspergillus niger== |
- | The line below this paragraph, containing "STRUCTURE_1uwc", creates the "Structure Box" on the page.
| + | <StructureSection load='1uwc' size='340' side='right'caption='[[1uwc]], [[Resolution|resolution]] 1.08Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1uwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UWC FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08Å</td></tr> |
- | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FER:3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC+ACID'>FER</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | {{STRUCTURE_1uwc| PDB=1uwc | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwc OCA], [https://pdbe.org/1uwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uwc RCSB], [https://www.ebi.ac.uk/pdbsum/1uwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwc ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/FAEA_ASPNG FAEA_ASPNG] Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.<ref>PMID:9406381</ref> <ref>PMID:11931668</ref> <ref>PMID:7805053</ref> <ref>PMID:9649839</ref> <ref>PMID:11931668</ref> <ref>PMID:15081808</ref> <ref>PMID:17027758</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uw/1uwc_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uwc ConSurf]. |
| + | <div style="clear:both"></div> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site. |
| | | |
- | ===FERULOYL ESTERASE FROM ASPERGILLUS NIGER===
| + | Structure of a feruloyl esterase from Aspergillus niger.,McAuley KE, Svendsen A, Patkar SA, Wilson KS Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:15103133<ref>PMID:15103133</ref> |
| | | |
- | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | <!--
| + | </div> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_15103133}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 1uwc" style="background-color:#fffaf0;"></div> |
- | (as it appears on PubMed at http://www.pubmed.gov), where 15103133 is the PubMed ID number.
| + | == References == |
- | -->
| + | <references/> |
- | {{ABSTRACT_PUBMED_15103133}}
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure== | + | |
- | 1UWC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWC OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | Structure of a feruloyl esterase from Aspergillus niger., McAuley KE, Svendsen A, Patkar SA, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103133 15103133]
| + | |
| [[Category: Aspergillus niger]] | | [[Category: Aspergillus niger]] |
- | [[Category: Feruloyl esterase]] | + | [[Category: Large Structures]] |
- | [[Category: Single protein]] | + | [[Category: McAuley KE]] |
- | [[Category: Mcauley, K E.]]
| + | [[Category: Patkar SA]] |
- | [[Category: Patkar, S A.]] | + | [[Category: Svendsen A]] |
- | [[Category: Svendsen, A.]] | + | [[Category: Wilson KS]] |
- | [[Category: Wilson, K S.]] | + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Serine esterase]]
| + | |
- | [[Category: Xylan degradation]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:32:39 2008''
| + | |
| Structural highlights
Function
FAEA_ASPNG Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site.
Structure of a feruloyl esterase from Aspergillus niger.,McAuley KE, Svendsen A, Patkar SA, Wilson KS Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:15103133[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Vries RP, Michelsen B, Poulsen CH, Kroon PA, van den Heuvel RH, Faulds CB, Williamson G, van den Hombergh JP, Visser J. The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides. Appl Environ Microbiol. 1997 Dec;63(12):4638-44. PMID:9406381
- ↑ de Vries RP, vanKuyk PA, Kester HC, Visser J. The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem J. 2002 Apr 15;363(Pt 2):377-86. PMID:11931668
- ↑ Ralet MC, Faulds CB, Williamson G, Thibault JF. Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger. Carbohydr Res. 1994 Oct 17;263(2):257-69. PMID:7805053
- ↑ Aliwan FO, Williamson G. Identification of active site residues in a ferulic acid esterase (FAE-III) from Aspergillus niger. Biochem Soc Trans. 1998 May;26(2):S164. PMID:9649839
- ↑ de Vries RP, vanKuyk PA, Kester HC, Visser J. The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem J. 2002 Apr 15;363(Pt 2):377-86. PMID:11931668
- ↑ Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB. The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family. J Mol Biol. 2004 Apr 30;338(3):495-506. PMID:15081808 doi:10.1016/j.jmb.2004.03.003
- ↑ Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C. Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A. FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:17027758 doi:10.1016/j.febslet.2006.09.039
- ↑ McAuley KE, Svendsen A, Patkar SA, Wilson KS. Structure of a feruloyl esterase from Aspergillus niger. Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:15103133 doi:10.1107/S0907444904004937
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