Three-dimensional structure of RBcel1, a metagenome-derived psychrotolerant family GH5 endoglucanase.

• Published in: Acta Crystallographica Section F Structural Biology and Crystallization Communications
• Main Authors: Delsaute, Maud, Berlemont, Renaud, Dehareng, Dominique, Van Elder, Dany, Galleni, Moreno, Bauvois, Cedric
• Format: Article in Journal/Newspaper
• Language: English
• Published: International Union of Crystallography 2013
• Subjects: Amino Acid Sequence; Binding Sites/physiology; Cellulase/chemistry/genetics; Crystallization; Glycoside Hydrolases/chemistry/genetics; Metagenome/genetics; Molecular Conformation; Molecular Sequence Data; Protein Structure; Secondary; Tertiary; bacterial cellulose synthesis; endoglucanases; family 5 glycosyl hydrolases; psychrotolerant; uncultured bacteria; Life sciences; Biochemistry; biophysics & molecular biology; Sciences du vivant; Biochimie; biophysique & biologie moléculaire; Antarctic; The Antarctic; Antarc*
• Online Access: https://orbi.uliege.be/handle/2268/188593; https://doi.org/10.1107/S1744309113014565

peer reviewed RBcel1 is an endoglucanase belonging to glycoside hydrolase family 5 subfamily 5 (GH5_5) that was recently identified from a soil metagenome library from the Antarctic. Unlike its closest structural homologue (Cel5A from Thermoascus aurantiacus), this enzyme was reported to be able to catalyze transglycosylation reactions and has putatively been implicated in the bacterial cellulose-synthesis process. Here, the structure of RBcel1 at 1.4 A resolution, solved by molecular replacement, is reported. The structure and putative substrate-binding site are described and compared with those of other GH5_5 subfamily members.