PDBsum entry: 1wb6

Hydrolase

PDB id: 1wb6

Contents

Protein chains

283 a.a. *

Ligands

VXX ×2

GOL ×7

ACT ×2

Metals

_CD ×20

Waters ×686

* Residue conservation analysis

PDB id:

1wb6

Name:

Hydrolase

Title:

S954a mutant of the feruloyl esterase module from clostridium thermocellum complexed with vanillate

Structure:

Endo-1,4-beta-xylanase y. Chain: a, b. Fragment: feruloyl esterase domain, residues 792-1077. Synonym: xylanase y, xyly, 1,4-beta-d-xylan xylanohydrolase xylanase xyn10b. Engineered: yes. Mutation: yes

Source:

Clostridium thermocellum. Organism_taxid: 1515. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.40Å R-factor: 0.118 R-free: 0.140

Authors:

N.Tarbouriech,J.A.Prates,C.Fontes,G.J.Davies

Key ref:

N.Tarbouriech et al. (2005). Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum. Acta Crystallogr D Biol Crystallogr, 61, 194-197. PubMed id: 15681871 DOI: 10.1107/S0907444904029695

Date:

30-Oct-04 Release date: 24-May-06

Protein chains

P51584  (XYNY_CLOTM) -  Endo-1,4-beta-xylanase Y

Seq: 1077 a.a.

Struc: 283 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.8 - Endo-1,4-beta-xylanase.
• Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.

DOI no: 10.1107/S0907444904029695

Acta Crystallogr D Biol Crystallogr 61:194-197 (2005)

PubMed id: 15681871

Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum.

N.Tarbouriech, J.A.Prates, C.M.Fontes, G.J.Davies.

ABSTRACT

Feruloyl esterases play a key role in the degradation of the intricate structure of the plant cell wall by hydrolysing the ferulate ester groups involved in the cross-linking between hemicelluloses and between hemicellulose and lignin. The structure of the feruloyl esterase module of Clostridium thermocellum cellulosomal xylanase 10B has been reported previously. It displays the alpha/beta hydrolase fold with a classical Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of this feruloyl esterase in complexes with methyl syringate, methyl sinapinate and methyl vanillate are described. Substrate binding is accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural determinants, particularly the m-methoxy substituent, governing the substrate specificity of Xyn10B feruloyl esterase are rationalized.

Selected figure(s)

Figure 3.
Figure 3 Superimposition of the active-site environment and substrates. Residues involved in movements are labelled as well as the catalytic triad. The methyl sinapinate complex is in orange, methyl vanillate in pink, methyl syringate in blue and the native uncomplexed structure in white. The figure was prepared using PyMOL (DeLano Scientific).

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 194-197) copyright 2005.

Figure was selected by an automated process.