Structural highlights
Publication Abstract from PubMed
The polysaccharide utilization locus in Bacteroides plebeius that confers the ability to catabolize porphyran contains a putative GH50 beta-agarase (BACPLE_01683, BpGH50). BpGH50 did not show any clear activity on agarose or on the related algal galactans porphyran and carrageenan. However, the 1.4 A resolution x-ray crystal structure of BpGH50 confirmed its possession of the core (alpha/beta)8 barrel fold found in GH50 enzymes as well as the structural conservation of the catalytic residues and some substrate binding residues. Examination of the structure supports assignment of this protein as a beta-galactosidase but suggests that it may utilize a different, possibly hybrid, algal galactan substrate. This article is protected by copyright. All rights reserved.
Structure of a glycoside hydrolase family 50 enzyme from a subfamily that is enriched in human gut microbiome Bacteroidetes.,Giles K, Pluvinage B, Boraston AB Proteins. 2016 Oct 18. doi: 10.1002/prot.25189. PMID:27756110[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Giles K, Pluvinage B, Boraston AB. Structure of a glycoside hydrolase family 50 enzyme from a subfamily that is enriched in human gut microbiome Bacteroidetes. Proteins. 2016 Oct 18. doi: 10.1002/prot.25189. PMID:27756110 doi:http://dx.doi.org/10.1002/prot.25189