2bjh
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2bjh.gif|left|200px]] | [[Image:2bjh.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2bjh", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_2bjh| PDB=2bjh | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''CRYSTAL STRUCTURE OF S133A ANFAEA-FERULIC ACID COMPLEX''' | '''CRYSTAL STRUCTURE OF S133A ANFAEA-FERULIC ACID COMPLEX''' | ||
Line 33: | Line 30: | ||
[[Category: Molina, R.]] | [[Category: Molina, R.]] | ||
[[Category: Sanz-Aparicio, J.]] | [[Category: Sanz-Aparicio, J.]] | ||
- | [[Category: | + | [[Category: Degradation plant cell wall]] |
- | [[Category: | + | [[Category: Feruloyl esterase]] |
- | [[Category: | + | [[Category: Glycoprotein]] |
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Serine esterase]] |
- | [[Category: | + | [[Category: Signal]] |
- | [[Category: | + | [[Category: Xylan degradation]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:22:30 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:22, 3 May 2008
CRYSTAL STRUCTURE OF S133A ANFAEA-FERULIC ACID COMPLEX
Overview
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.
About this Structure
2BJH is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 20:22:30 2008