2025/05/19 by Emily Knudson-Goerner, A.B. Boraston · 1 voice
Biochemistry, Genetics and Molecular Biology · Nursing · Engineering · #Enzyme Production and Characterization #Microbial Metabolites in Food Biotechnology #Biofuel production and bioconversion
paper · pdf · doi:10.1107/s2053230x2500425x
openalex publication_date 2025/05/19 · openalex created_date 2025/05/27 · openalex updated_date 2026/07/25
The genome of the marine bacterium Muricauda eckloniae sp. DK169 contains an extensive polysaccharide-utilization locus that targets fucoidan from brown algae. Within this locus is a gene that encodes a putative fucoidan-degrading glycoside hydrolase (locus tag AAY4201205) assigned to glycoside hydrolase family 168, which we call Me GH168. We present the 2.0 Å resolution X-ray crystal structure of Me GH168, demonstrating a (β/α) 8 -barrel fold. The eight loop regions joining each α-helix and β-strand surround the catalytic groove. A comparison with the structure of a GH168, Fun168A, in complex with a fragment of fucoidan (PDB entry 8ya7) revealed conservation of key residues in the catalytic site. However, structural variation in positive-subsite loop regions may recontour the active site to create differences in substrate specificity between the two GH168s. The present data provide additional structural insights into the GH168 family, particularly expanding on sequence and structure conservation (and the lack thereof) in relation to substrate interactions.