Title : The Structure of the Feruloyl Esterase Module of Xylanase 10B from Clostridium thermocellum Provides Insights into Substrate Recognition - Prates_2001_Structure_9_1183 |
Author(s) : Prates JA , Tarbouriech N , Charnock SJ , Fontes CM , Ferreira LM , Davies GJ |
Ref : Structure , 9 :1183 , 2001 |
Abstract :
BACKGROUND:
Degradation of the plant cell wall requires the synergistic action of a consortium of predominantly modular enzymes. In Clostridiae, these biocatalysts are organized into a supramolecular assembly termed a "cellulosome." This multienzyme complex possesses, in addition to its well-described cellulolytic activity, an apparatus specific for xylan degradation. Cinnamic acid esterases hydrolyze the ferulate groups involved in the crosslinking of arabinoxylans to lignin and thus play a key role in the degradation of the plant cell wall in addition to having promising industrial and medical applications.
RESULTS:
We have cloned and overexpressed the feruloyl esterase module from a 5 domain xylanase, Xyn10B from Clostridium thermocellum. The native structure at 1.6 A resolution has been solved with selenomethionine multiple wavelength anomalous dispersion and refined to a final R(free) of 17.8%. The structure of a hydrolytically inactive mutant, S954A, in complex with the reaction product ferulic acid has been refined at a resolution of 1.4 A with an R(free) of 16.0%.
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PubMedSearch : Prates_2001_Structure_9_1183 |
PubMedID: 11738044 |
Gene_locus related to this paper: clotm-xyny |
Mutation | S954A_clotm-xyny |
Substrate | Ferulic-acid Methyl-sinapate |
Gene_locus | clotm-xyny |
Family | A85-Feruloyl-Esterase |
Structure | 1GKK 1GKL 1WB4 |
Prates JA, Tarbouriech N, Charnock SJ, Fontes CM, Ferreira LM, Davies GJ (2001)
The Structure of the Feruloyl Esterase Module of Xylanase 10B from Clostridium thermocellum Provides Insights into Substrate Recognition
Structure
9 :1183
Prates JA, Tarbouriech N, Charnock SJ, Fontes CM, Ferreira LM, Davies GJ (2001)
Structure
9 :1183