4g4i

Crystal structure of glucuronoyl esterase S213A mutant from Sporotrichum thermophile determined at 1.9 A resolution

spinqualitylabelsall models 4g4i, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g4i is a 1 chain structure with sequence from Thermothelomyces thermophilus ATCC 42464. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GCE2_MYCTT Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. Publication Abstract from PubMed The increasing demand for the development of efficient biocatalysts is a consequence of their broad industrial applications. Typical difficulties that are encountered during their exploitation in a variety of processes are interconnected with factors such as temperature, pH, product inhibitors etc. To eliminate these, research has been directed towards the identification of new enzymes that would comply with the required standards. To this end, the recently discovered glucuronoyl esterases (GEs) are an enigmatic family within the carbohydrate esterase (CE) family. Structures of the thermophilic StGE2 esterase from Myceliophthora thermophila (synonym Sporotrichum thermophile), a member of the CE15 family, and its S213A mutant were determined at 1.55 and 1.9 A resolution, respectively. The first crystal structure of the S213A mutant in complex with a substrate analogue, methyl 4-O-methyl-beta-D-glucopyranuronate, was determined at 2.35 A resolution. All of the three-dimensional protein structures have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. These are the first crystal structures of a thermophilic GE both in an unliganded form and bound to a substrate analogue, thus unravelling the organization of the catalytic triad residues and their neighbours lining the active site. The knowledge derived offers novel insights into the key structural elements that drive the hydrolysis of glucuronic acid esters. The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst.,Charavgi MD, Dimarogona M, Topakas E, Christakopoulos P, Chrysina ED Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):63-73. doi:, 10.1107/S0907444912042400. Epub 2012 Dec 20. PMID:23275164 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methylesterase 3D structures

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