1gkl
S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH FERULIC ACID
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OverviewOverview
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, ... [(full description)]
About this StructureAbout this Structure
1GKL is a [Single protein] structure of sequence from [Clostridium thermocellum] with CD, FER, GOL and ACY as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: FEA. Full crystallographic information is available from [OCA].
ReferenceReference
The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition., Prates JA, Tarbouriech N, Charnock SJ, Fontes CM, Ferreira LM, Davies GJ, Structure. 2001 Dec;9(12):1183-90. PMID:11738044
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