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2bjh

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Revision as of 06:08, 16 May 2018

Crystal Structure Of S133A AnFaeA-ferulic acid complex

Structural highlights

2bjh is a 3 chain structure with sequence from A. niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1usw, 1uwc, 1uza
Activity:	Feruloyl esterase, with EC number 3.1.1.73
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Feruloyl esterases hydrolyse 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 glycoside hydrolases. Here we describe the crystal structure of inactive S133A mutant of type-A feruloyl esterase from Aspergillus niger (AnFaeA) in complex with a feruloylated trisaccharide substrate. Only the ferulic acid moiety of the substrate is visible in the electron density map, showing interactions through its OH and OCH(3) groups with the hydroxyl groups of Tyr80. The importance of aromatic and polar residues in the activity of AnFaeA was also evaluated using site-directed mutagenesis. Four mutant proteins were heterologously expressed in Pichia pastoris, and their kinetic properties determined against methyl esters of ferulic, sinapic, caffeic and p-coumaric acid. The k(cat) of Y80S, Y80V, W260S and W260V was drastically reduced compared to that of the wild-type enzyme. However, the replacement of Tyr80 and Trp260 with smaller residues broadened the substrate specificity of the enzyme, allowing the hydrolysis of methyl caffeate. The role of Tyr80 and Trp260 in AnFaeA are discussed in light of the three-dimensional structure.

Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger.,Faulds CB, Molina R, Gonzalez R, Husband F, Juge N, Sanz-Aparicio J, Hermoso JA FEBS J. 2005 Sep;272(17):4362-71. PMID:16128806^[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
↑ Faulds CB, Molina R, Gonzalez R, Husband F, Juge N, Sanz-Aparicio J, Hermoso JA. Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger. FEBS J. 2005 Sep;272(17):4362-71. PMID:16128806 doi:10.1111/j.1742-4658.2005.04849.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bjh"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF S133A ANFAEA-FERULIC ACID COMPLEX==
+==Crystal Structure Of S133A AnFaeA-ferulic acid complex==
 <StructureSection load='2bjh' size='340' side='right' caption='[[2bjh]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1usw|1usw]], [[1uwc|1uwc]], [[1uza|1uza]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjh OCA], [http://pdbe.org/2bjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bjh RCSB], [http://www.ebi.ac.uk/pdbsum/2bjh PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjh OCA], [http://pdbe.org/2bjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bjh RCSB], [http://www.ebi.ac.uk/pdbsum/2bjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/2bjh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/2bjh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2bjh

From Proteopedia

Revision as of 06:08, 16 May 2018

Crystal Structure Of S133A AnFaeA-ferulic acid complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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