Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst
Δημιουργός/Συγγραφέας:	Charavgi M.-D. Dimarogona M. Topakas E. Christakopoulos P. [EL] Χρυσίνα, Ευαγγελία Δ.[EN] Chrysina, Evangelia D.
Ημερομηνία:	2013
Γλώσσα:	Αγγλικά
ISSN:	0907-4449
DOI:	10.1107/S0907444912042400
Άλλο:	PubMed ID: 23275164
Περίληψη:	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 Å resolution, respectively. The first crystal structure of the S213A mutant in complex with a substrate analogue, methyl 4-O-methyl-Β-d-glucopyranuronate, was determined at 2.35 Å resolution. All of the three-dimensional protein structures have an /Β-hydrolase fold with a three-layer Β-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.
Τίτλος πηγής δημοσίευσης:	Acta Crystallographica Section D: Biological Crystallography
Τόμος/Κεφάλαιο:	69
Τεύχος:	1
Σελίδες:	63-73
Θεματική Κατηγορία:	[EL] Βιολογία (Γενικά)[EN] Biology (General) [EL] Χημεία (Γενικά)[EN] Chemistry (General)
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Όροι και προϋποθέσεις δικαιωμάτων:	All Open Access, Green
Σημειώσεις:	Seventh Framework Programme, FP7: 226716, 230146, 245866
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο