Title : Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum - Tarbouriech_2005_Acta.Crystallogr.D.Biol.Crystallogr_61_194 |
Author(s) : Tarbouriech N , Prates JA , Fontes CM , Davies GJ |
Ref : Acta Crystallographica D Biol Crystallogr , 61 :194 , 2005 |
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. |
PubMedSearch : Tarbouriech_2005_Acta.Crystallogr.D.Biol.Crystallogr_61_194 |
PubMedID: 15681871 |
Gene_locus related to this paper: clotm-xyny |
Mutation | S954A_clotm-xyny |
Substrate | Sinapinic-acid Methyl-vanillate Methyl-syringate Methyl-sinapate |
Gene_locus | clotm-xyny |
Family | Antigen85c A85-Feruloyl-Esterase |
Structure | 1WB4 1WB5 1WB6 |
Tarbouriech N, Prates JA, Fontes CM, Davies GJ (2005)
Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum
Acta Crystallographica D Biol Crystallogr
61 :194
Tarbouriech N, Prates JA, Fontes CM, Davies GJ (2005)
Acta Crystallographica D Biol Crystallogr
61 :194