1GKK

Feruloyl esterase domain of XynY from clostridium thermocellum

Summary for 1GKK

• Entry DOI: 10.2210/pdb1gkk/pdb
• Related: 1DYO 1GKL 1H6X 1H6Y
• Descriptor: ENDO-1,4-BETA-XYLANASE Y, CADMIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hydrolase, ferulic acid, esterase family 1
• Biological source: CLOSTRIDIUM THERMOCELLUM
• Total number of polymer chains: 2
• Total formula weight: 69749.33

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: 2011-09-07)

Primary citation

Prates, J.A.M.,Tarbouriech, N.,Charnock, S.J.,Fontes, C.M.G.A.,Ferreira, L.M.A.,Davies, G.J.
The Structure of the Feruloyl Esterase Module of Xylanase 10B from Clostridium Thermocellum Provides Insights Into Substrate Recognition
Structure, 9:1183-, 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 (1.6 Å)