8RG5
Crystal structure of PbFucA from Planctomycetes bacterium K23_9 in P 4 21 2
Summary for 8RG5
Entry DOI | 10.2210/pdb8rg5/pdb |
Descriptor | Glycoside-hydrolase family GH114 TIM-barrel domain-containing protein, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total) |
Functional Keywords | fucoidan, endo-fucoidanase, endo-fucanase, gh168, glycosyl hydrolase, hydrolase |
Biological source | Planctomycetes bacterium K23_9 |
Total number of polymer chains | 2 |
Total formula weight | 82938.09 |
Authors | Perez-Cruz, C.,Moraleda-Montoya, A.,Liebana, R.,Lorizate, M.,Arrizabalaga, U.,Garcia-Alija, M.,Terrones, O.,Contreras, F.X.,Guerin, M.E.,Trastoy, B.,Alonso-Saez, L. (deposition date: 2023-12-13, release date: 2025-01-01, Last modification date: 2025-01-08) |
Primary citation | Perez-Cruz, C.,Moraleda-Montoya, A.,Liebana, R.,Terrones, O.,Arrizabalaga, U.,Garcia-Alija, M.,Lorizate, M.,Martinez Gascuena, A.,Garcia-Alvarez, I.,Nieto-Garai, J.A.,Olazar-Intxausti, J.,Rodriguez-Colinas, B.,Mann, E.,Chiara, J.L.,Contreras, F.X.,Guerin, M.E.,Trastoy, B.,Alonso-Saez, L. Mechanisms of recalcitrant fucoidan breakdown in marine Planctomycetota. Nat Commun, 15:10906-10906, 2024 Cited by PubMed Abstract: Marine brown algae produce the highly recalcitrant polysaccharide fucoidan, contributing to long-term oceanic carbon storage and climate regulation. Fucoidan is degraded by specialized heterotrophic bacteria, which promote ecosystem function and global carbon turnover using largely uncharacterized mechanisms. Here, we isolate and study two Planctomycetota strains from the microbiome associated with the alga Fucus spiralis, which grow efficiently on chemically diverse fucoidans. One of the strains appears to internalize the polymer, while the other strain degrades it extracellularly. Multi-omic approaches show that fucoidan breakdown is mediated by the expression of divergent polysaccharide utilization loci, and endo-fucanases of family GH168 are strongly upregulated during fucoidan digestion. Enzymatic assays and structural biology studies reveal how GH168 endo-fucanases degrade various fucoidan cores from brown algae, assisted by auxiliary hydrolytic enzymes. Overall, our results provide insights into fucoidan processing mechanisms in macroalgal-associated bacteria. PubMed: 39738071DOI: 10.1038/s41467-024-55268-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.18 Å) |
Structure validation
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