1WB5

S954A mutant of the feruloyl esterase module from clostridium thermocellum complexed with syringate

Summary for 1WB5

• Entry DOI: 10.2210/pdb1wb5/pdb
• Related: 1DYO 1GKK 1GKL 1H6X 1H6Y 1OHZ 1WB4 1WB6
• Descriptor: ENDO-1,4-BETA-XYLANASE Y, SYRINGATE, GLYCEROL, ... (6 entities in total)
• Functional Keywords: esterase family 1, ferulic acid, glycosidase, hydrolase, xylan degradation, xylanase
• Biological source: CLOSTRIDIUM THERMOCELLUM
• Total number of polymer chains: 2
• Total formula weight: 70318.93

Authors

Tarbouriech, N.,Prates, J.A.,Fontes, C.,Davies, G.J. (deposition date: 2004-10-30, release date: 2005-02-02, Last modification date: 2023-12-13)

Primary citation

Tarbouriech, N.,Prates, J.A.,Fontes, C.,Davies, G.J.
Molecular Determinants of Substrate Specificity in the Feruloyl Esterase Module of Xylanase 10B from Clostridium Thermocellum
Acta Crystallogr.,Sect.D, 61:194-, 2005

PubMed 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.

PubMed: 15681871
DOI: 10.1107/S0907444904029695

Experimental method

X-RAY DIFFRACTION (1.4 Å)