6GL2

Structure of ZgEngAGH5_4 wild type at 1.2 Angstrom resolution

Summary for 6GL2

• Entry DOI: 10.2210/pdb6gl2/pdb
• Descriptor: Endoglucanase, family GH5, IMIDAZOLE (3 entities in total)
• Functional Keywords: glycoside hydrolase, gh5, mixed linked glucan, zobellia galactanivorans, hydrolase
• Biological source: Zobellia galactanivorans
• Total number of polymer chains: 1
• Total formula weight: 38576.91

Authors

Dorival, J.,Ruppert, S.,Gunnoo, M.,Orlowski, A.,Chapelais, M.,Dabin, J.,Labourel, A.,Thompson, D.,Michel, G.,Czjzek, M.,Genicot, S. (deposition date: 2018-05-22, release date: 2018-10-31, Last modification date: 2024-01-17)

Primary citation

Dorival, J.,Ruppert, S.,Gunnoo, M.,Orlowski, A.,Chapelais-Baron, M.,Dabin, J.,Labourel, A.,Thompson, D.,Michel, G.,Czjzek, M.,Genicot, S.
The laterally acquired GH5ZgEngAGH5_4from the marine bacteriumZobellia galactanivoransis dedicated to hemicellulose hydrolysis.
Biochem. J., 475:3609-3628, 2018

PubMed Abstract: Cell walls of marine macroalgae are composed of diverse polysaccharides that provide abundant carbon sources for marine heterotrophic bacteria. Among them, is considered as a model for studying algae-bacteria interactions. The degradation of typical algal polysaccharides, such as agars or alginate, has been intensively studied in this model bacterium, but the catabolism of plant-like polysaccharides is essentially uncharacterized. Here, we identify a polysaccharide utilization locus in the genome of , induced by laminarin (β-1,3-glucans), and containing a putative GH5 subfamily 4 (GH5_4) enzyme, currently annotated as a endoglucanase (EngA). A phylogenetic analysis indicates that EngA was laterally acquired from an ancestral We performed the biochemical and structural characterization of EngA and demonstrated that this GH5 is, in fact, an endo-β-glucanase, most active on mixed-linked glucan (MLG). Although EngA and GH16 lichenases both hydrolyze MLG, these two types of enzymes release different series of oligosaccharides. Structural analyses of EngA reveal that all the amino acid residues involved in the catalytic triad and in the negative glucose-binding subsites are conserved, when compared with the closest relative, the cellulase EngD from , and some other GH5s. In contrast, the positive glucose-binding subsites of EngA are different and this could explain the preference for MLG, with respect to cellulose or laminarin. Molecular dynamics computer simulations using different hexaoses reveal that the specificity for MLG occurs through the +1 and +2 subsites of the binding pocket that display the most important differences when compared with the structures of other GH5_4 enzymes.

PubMed: 30341165
DOI: 10.1042/BCJ20180486

Experimental method

X-RAY DIFFRACTION (1.96 Å)