2UY5

ScCTS1_kinetin crystal structure

Summary for 2UY5

• Entry DOI: 10.2210/pdb2uy5/pdb
• Related: 2UY2 2UY3 2UY4
• Descriptor: ENDOCHITINASE, N-(FURAN-2-YLMETHYL)-7H-PURIN-6-AMINE (3 entities in total)
• Functional Keywords: carbohydrate metabolism, polysaccharide degradation, chitinase, glycoside hydrolase family 18, chitin-binding, chitin degradation, cazy, hydrolase, glycosidase
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Secreted: P29029
• Total number of polymer chains: 1
• Total formula weight: 31745.44

Authors

Hurtado-Guerrero, R.,van Aalten, D.M.F. (deposition date: 2007-04-02, release date: 2007-04-24, Last modification date: 2024-10-23)

Primary citation

Hurtado-Guerrero, R.,Van Aalten, D.M.F.
Structure of Saccharomyces Cerevisiae Chitinase 1 and Screening-Based Discovery of Potent Inhibitors.
Chem.Biol., 14:589-, 2007

PubMed Abstract: Chitinases hydrolyse the beta(1,4)-glycosidic bonds of chitin, an essential fungal cell wall component. Genetic data on a subclass of fungal family 18 chitinases have suggested a role in cell wall morphology. Specific inhibitors of these enzymes would be useful as tools to study their role in cell wall morphogenesis and could possess antifungal properties. Here, we describe the crystallographic structure of a fungal "plant-type" family 18 chitinase, that of Saccharomyces cerevisiae CTS1. The enzyme is active against 4-methylumbelliferyl chitooligosaccharides and displays an unusually low pH optimum for activity. A library screen against ScCTS1 yielded hits with Ki 's as low as 3.2 microM. Crystal structures of ScCTS1 in complex with inhibitors from three series reveal striking mimicry of carbohydrate substrate by small aromatic moieties and a pocket that could be further exploited in optimization of these inhibitors.

PubMed: 17524989
DOI: 10.1016/J.CHEMBIOL.2007.03.015

Experimental method

X-RAY DIFFRACTION (1.6 Å)