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| - | [[Image:1uwc.gif|left|200px]]<br /><applet load="1uwc" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1uwc, resolution 1.08Å" /> | |
| - | '''FERULOYL ESTERASE FROM ASPERGILLUS NIGER'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Feruloyl esterase from Aspergillus niger== |
| - | 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. | + | <StructureSection load='1uwc' size='340' side='right'caption='[[1uwc]], [[Resolution|resolution]] 1.08Å' scene=''> |
| | + | == Structural highlights == |
| | + | <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> |
| | + | </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> |
| | + | <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. |
| | | | |
| - | ==About this Structure==
| + | 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> |
| - | 1UWC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with NAG, SO4 and FER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Feruloyl_esterase Feruloyl esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.73 3.1.1.73] Known structural/functional Site: <scene name='pdbsite=AC1:Fer Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UWC OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15103133 15103133]
| + | </div> |
| | + | <div class="pdbe-citations 1uwc" style="background-color:#fffaf0;"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[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: FER]]
| + | |
| - | [[Category: NAG]]
| + | |
| - | [[Category: SO4]]
| + | |
| - | [[Category: hydrolase]]
| + | |
| - | [[Category: serine esterase]]
| + | |
| - | [[Category: xylan degradation]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:14:19 2007''
| + | |
| 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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