|
|
| (16 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:1usw.jpg|left|200px]]<br /><applet load="1usw" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1usw, resolution 2.5Å" /> | |
| - | '''CRYSTAL STRUCTURE OF FERULIC ACID ESTERASE FROM ASPERGILLUS NIGER'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Crystal Structure of Ferulic Acid Esterase from Aspergillus niger== |
| - | As a component of the array of enzymes produced by micro-organisms to, deconstruct plant cell walls, feruloyl esterases hydrolyze phenolic groups, involved in the cross-linking of arabinoxylan to other polymeric, structures. This is important for opening the cell wall structure, making, material more accessible to glycosyl hydrolases. Here, we describe the, first crystal structure of the non-modular type-A feruloyl esterase from, Aspergillus niger (AnFaeA) solved at 2.5A resolution. AnFaeA displays an, alpha/beta hydrolase fold similar to that found in fungal lipases and, different from that reported for other feruloyl esterases., Crystallographic and site-directed mutagenesis studies allow us to, identify the catalytic triad (Ser133-His247-Asp194) that forms the, catalytic machinery of this enzyme. The active-site cavity is confined by, a lid (residues 68-80), on the analogy of lipases, and by a loop (residues, 226-244) that confers plasticity to the substrate-binding site. The lid, presents a high ratio of polar residues, which in addition to a unique, N-glycosylation site stabilises the lid in an open conformation, conferring the esterase character to this enzyme. A putative model for, bound 5,5'-diferulic acid-linked arabinoxylan has been built, pointing to, the more relevant residues involved in substrate recognition. Comparison, with structurally related lipases reveals that subtle amino acid and, conformational changes within a highly conserved protein fold may produce, protein variants endowed with new enzymatic properties, while comparison, with functionally related proteins points to a functional convergence, after evolutionary divergence within the feruloyl esterases family. | + | <StructureSection load='1usw' size='340' side='right'caption='[[1usw]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1usw]] is a 1 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=1USW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USW 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]] 2.5Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1usw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usw OCA], [https://pdbe.org/1usw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1usw RCSB], [https://www.ebi.ac.uk/pdbsum/1usw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1usw 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/us/1usw_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1usw ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | As a component of the array of enzymes produced by micro-organisms to deconstruct plant cell walls, feruloyl esterases hydrolyze phenolic groups involved in the cross-linking of arabinoxylan to other polymeric structures. This is important for opening the cell wall structure, making material more accessible to glycosyl hydrolases. Here, we describe the first crystal structure of the non-modular type-A feruloyl esterase from Aspergillus niger (AnFaeA) solved at 2.5A resolution. AnFaeA displays an alpha/beta hydrolase fold similar to that found in fungal lipases and different from that reported for other feruloyl esterases. Crystallographic and site-directed mutagenesis studies allow us to identify the catalytic triad (Ser133-His247-Asp194) that forms the catalytic machinery of this enzyme. The active-site cavity is confined by a lid (residues 68-80), on the analogy of lipases, and by a loop (residues 226-244) that confers plasticity to the substrate-binding site. The lid presents a high ratio of polar residues, which in addition to a unique N-glycosylation site stabilises the lid in an open conformation, conferring the esterase character to this enzyme. A putative model for bound 5,5'-diferulic acid-linked arabinoxylan has been built, pointing to the more relevant residues involved in substrate recognition. Comparison with structurally related lipases reveals that subtle amino acid and conformational changes within a highly conserved protein fold may produce protein variants endowed with new enzymatic properties, while comparison with functionally related proteins points to a functional convergence after evolutionary divergence within the feruloyl esterases family. |
| | | | |
| - | ==About this Structure==
| + | The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family.,Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB J Mol Biol. 2004 Apr 30;338(3):495-506. PMID:15081808<ref>PMID:15081808</ref> |
| - | 1USW 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 <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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:Nag+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USW OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family., Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB, J Mol Biol. 2004 Apr 30;338(3):495-506. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15081808 15081808]
| + | </div> |
| | + | <div class="pdbe-citations 1usw" 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: Faulds C]] |
| - | [[Category: Faulds, C.]] | + | [[Category: Hermoso J]] |
| - | [[Category: Hermoso, J.]] | + | [[Category: Molina R]] |
| - | [[Category: Molina, R.]] | + | [[Category: Sanz-Aparicio J]] |
| - | [[Category: Sanz-Aparicio, J.]] | + | |
| - | [[Category: SO4]]
| + | |
| - | [[Category: degradation plant cell walls]]
| + | |
| - | [[Category: feruloyl esterase]]
| + | |
| - | [[Category: hydrolase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:04:32 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
As a component of the array of enzymes produced by micro-organisms to deconstruct plant cell walls, feruloyl esterases hydrolyze phenolic groups involved in the cross-linking of arabinoxylan to other polymeric structures. This is important for opening the cell wall structure, making material more accessible to glycosyl hydrolases. Here, we describe the first crystal structure of the non-modular type-A feruloyl esterase from Aspergillus niger (AnFaeA) solved at 2.5A resolution. AnFaeA displays an alpha/beta hydrolase fold similar to that found in fungal lipases and different from that reported for other feruloyl esterases. Crystallographic and site-directed mutagenesis studies allow us to identify the catalytic triad (Ser133-His247-Asp194) that forms the catalytic machinery of this enzyme. The active-site cavity is confined by a lid (residues 68-80), on the analogy of lipases, and by a loop (residues 226-244) that confers plasticity to the substrate-binding site. The lid presents a high ratio of polar residues, which in addition to a unique N-glycosylation site stabilises the lid in an open conformation, conferring the esterase character to this enzyme. A putative model for bound 5,5'-diferulic acid-linked arabinoxylan has been built, pointing to the more relevant residues involved in substrate recognition. Comparison with structurally related lipases reveals that subtle amino acid and conformational changes within a highly conserved protein fold may produce protein variants endowed with new enzymatic properties, while comparison with functionally related proteins points to a functional convergence after evolutionary divergence within the feruloyl esterases family.
The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family.,Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB J Mol Biol. 2004 Apr 30;338(3):495-506. PMID:15081808[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
- ↑ 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
|
