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| - | {{Seed}} | |
| - | [[Image:2ix9.png|left|200px]] | |
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| - | <!-- | + | ==Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A== |
| - | The line below this paragraph, containing "STRUCTURE_2ix9", creates the "Structure Box" on the page.
| + | <StructureSection load='2ix9' size='340' side='right'caption='[[2ix9]], [[Resolution|resolution]] 1.70Å' 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'>[[2ix9]] 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=2IX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX9 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]] 1.7Å</td></tr> |
| - | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | {{STRUCTURE_2ix9| PDB=2ix9 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix9 OCA], [https://pdbe.org/2ix9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix9 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/ix/2ix9_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=2ix9 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | The thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied. From the most to the least thermo-resistant, the four molecular species ranked as follows: (i) glycosylated form produced native, (ii) non-glycosylated form produced native, (iii) non-glycosylated form produced as inclusion bodies and refolded, and (iv) glycosylated form produced native chemically denatured and then refolded. On the basis of these results and of crystal structure data, we discuss the respective importance of protein folding and glycosylation in the thermal stability of recombinant FAEA. |
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| - | ===RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A===
| + | Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.,Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:17027758<ref>PMID:17027758</ref> |
| | | | |
| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_17027758}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 2ix9" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 17027758 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_17027758}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | |
| - | 2IX9 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=2IX9 OCA].
| + | |
| - | | + | |
| - | ==Reference== | + | |
| - | Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A., Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C, FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17027758 17027758]
| + | |
| | [[Category: Aspergillus niger]] | | [[Category: Aspergillus niger]] |
| - | [[Category: Feruloyl esterase]] | + | [[Category: Large Structures]] |
| - | [[Category: Single protein]]
| + | [[Category: Benoit I]] |
| - | [[Category: Benoit, I.]] | + | [[Category: Sulzenbacher G]] |
| - | [[Category: Sulzenbacher, G.]] | + | |
| - | [[Category: Feruloyl esterase ec 3 1.1 73]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine esterase]]
| + | |
| - | [[Category: Xylan degradation]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:57:05 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 thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied. From the most to the least thermo-resistant, the four molecular species ranked as follows: (i) glycosylated form produced native, (ii) non-glycosylated form produced native, (iii) non-glycosylated form produced as inclusion bodies and refolded, and (iv) glycosylated form produced native chemically denatured and then refolded. On the basis of these results and of crystal structure data, we discuss the respective importance of protein folding and glycosylation in the thermal stability of recombinant FAEA.
Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.,Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:17027758[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
- ↑ 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
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