PDBsum entry 1uwc

Hydrolase

PDB id

1uwc

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Contents

			Protein chains

					261 a.a. *

			Ligands

					NAG ×2


					FER ×3


					SO4 ×2

			Waters ×713

* Residue conservation analysis

PDB id:

1uwc

Links

Name:

Hydrolase

Title:

Feruloyl esterase from aspergillus niger

Structure:

Feruloyl esterase a. Chain: a, b. Synonym: ferulic acid esterase a, fae-iii, cinnamoyl esterase. Engineered: yes. Other_details: n-acetylglucosamine at asn 79

Source:

Aspergillus niger. Organism_taxid: 5061. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062

Resolution:

1.08Å

R-factor:

0.116

R-free:

0.138

Authors:

K.E.Mcauley,A.Svendsen,S.A.Patkar,K.S.Wilson

Key ref:

K.E.McAuley et al. (2004). Structure of a feruloyl esterase from Aspergillus niger. Acta Crystallogr D Biol Crystallogr, 60, 878-887. PubMed id: 15103133 DOI: 10.1107/S0907444904004937

Date:

03-Feb-04

Release date:

06-May-04

PROCHECK

	Headers

	References

Protein chains

O42807 (FAEA_ASPNG) - Feruloyl esterase A from Aspergillus niger

Seq: Struc:					281 a.a. 261 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.3.1.1.73 - feruloyl esterase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

feruloyl-polysaccharide + H2O = ferulate + polysaccharide

feruloyl-polysaccharide

H2O

ferulate
Bound ligand (Het Group name = FER)
corresponds exactly

polysaccharide

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1107/S0907444904004937	Acta Crystallogr D Biol Crystallogr 60:878-887 (2004)
PubMed id: 15103133

Structure of a feruloyl esterase from Aspergillus niger.
K.E.McAuley, A.Svendsen, S.A.Patkar, K.S.Wilson.

ABSTRACT

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.

Selected figure(s)



	Figure 1. Figure 1 Structure of arabinoxylan. The inset shows one type of ferulic acid dimer that can be formed.		Figure 2. Figure 2 Diagrams of (a) open-form TlL, (b) FAE-III and (c) closed-form TlL. The ribbon diagrams on the left are coloured yellow for -sheet, red for -helices and violet for the lid helix. On the right are the solvent-accessible surface representations. The surface is coloured by residue type: blue, basic; red, acidic; yellow, polar; grey, hydrophobic; green, catalytic triad. Figs. 2, 4, 5(b) and 6 were produced using PyMOL (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System. http://www.pymol.org .]).

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20801026

S.B.Zhang, and Z.L.Wu (2011).
Identification of amino acid residues responsible for increased thermostability of feruloyl esterase A from Aspergillus niger using the PoPMuSiC algorithm.

Bioresour Technol, 102, 2093-2096.

19644688

T.Koseki, S.Fushinobu, Ardiansyah, H.Shirakawa, and M.Komai (2009).
Occurrence, properties, and applications of feruloyl esterases.

Appl Microbiol Biotechnol, 84, 803-810.

18765911

Y.Sun, M.Li, Y.Zhang, L.Liu, Y.Liu, Z.Liu, X.Li, and Z.Lou (2008).
Crystallization and preliminary crystallographic analysis of Gibberella zeae extracellular lipase.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 813-815.

17092334

A.Levasseur, P.Gouret, L.Lesage-Meessen, M.Asther, M.Asther, E.Record, and P.Pontarotti (2006).
Tracking the connection between evolutionary and functional shifts using the fungal lipase/feruloyl esterase A family.

BMC Evol Biol, 6, 92.

16431911

E.J.Taylor, T.M.Gloster, J.P.Turkenburg, F.Vincent, A.M.Brzozowski, C.Dupont, F.Shareck, M.S.Centeno, J.A.Prates, V.Puchart, L.M.Ferreira, C.M.Fontes, P.Biely, and G.J.Davies (2006).
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases.

J Biol Chem, 281, 10968-10975.

PDB codes:

2c71 2c79 2cc0

17031032

T.Koseki, K.Takahashi, T.Handa, Y.Yamane, S.Fushinobu, and K.Hashizume (2006).
N-linked oligosaccharides of Aspergillus awamori feruloyl esterase are important for thermostability and catalysis.

Biosci Biotechnol Biochem, 70, 2476-2480.

16128806

C.B.Faulds, R.Molina, R.Gonzalez, F.Husband, N.Juge, J.Sanz-Aparicio, and J.A.Hermoso (2005).
Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger.

FEBS J, 272, 4362-4371.

PDB code:

2bjh

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.