1GKL

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

Summary for 1GKL

• Entry DOI: 10.2210/pdb1gkl/pdb
• Related: 1DYO 1GKK 1H6X 1H6Y
• Descriptor: ENDO-1,4-BETA-XYLANASE Y, 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID, GLYCEROL, ... (6 entities in total)
• Functional Keywords: hydrolase, esterase family 1, inactive mutant
• Biological source: CLOSTRIDIUM THERMOCELLUM
• Total number of polymer chains: 2
• Total formula weight: 69720.84

Authors

Prates, J.A.M.,Tarbouriech, N.,Charnock, S.J.,Fontes, C.M.G.A.,Ferreira, L.M.A.,Davies, G.J. (deposition date: 2001-08-15, release date: 2001-12-13, Last modification date: 2024-05-08)

Primary citation

Prates, J.A.,Tarbouriech, N.,Charnock, S.J.,Fontes, C.M.,Ferreira, L.M.,Davies, G.J.
The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition.
Structure, 9:1183-1190, 2001

PubMed Abstract: 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.

PubMed: 11738044
DOI: 10.1016/s0969-2126(01)00684-0

Experimental method

X-RAY DIFFRACTION (1.4 Å)