6HR5
Structure of the S1_25 family sulfatase module of the rhamnosidase FA22250 from Formosa agariphila
Summary for 6HR5
| Entry DOI | 10.2210/pdb6hr5/pdb |
| Descriptor | Alpha-L-rhamnosidase/sulfatase (GH78), CALCIUM ION (2 entities in total) |
| Functional Keywords | algal polysaccharide carrageenan sulfatase, hydrolase |
| Biological source | Formosa agariphila KMM 3901 |
| Total number of polymer chains | 1 |
| Total formula weight | 54378.94 |
| Authors | Roret, T.,Prechoux, A.,Czjzek, M.,Michel, G. (deposition date: 2018-09-26, release date: 2019-06-26, Last modification date: 2024-05-15) |
| Primary citation | Reisky, L.,Prechoux, A.,Zuhlke, M.K.,Baumgen, M.,Robb, C.S.,Gerlach, N.,Roret, T.,Stanetty, C.,Larocque, R.,Michel, G.,Song, T.,Markert, S.,Unfried, F.,Mihovilovic, M.D.,Trautwein-Schult, A.,Becher, D.,Schweder, T.,Bornscheuer, U.T.,Hehemann, J.H. A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. Nat.Chem.Biol., 15:803-812, 2019 Cited by PubMed Abstract: Marine seaweeds increasingly grow into extensive algal blooms, which are detrimental to coastal ecosystems, tourism and aquaculture. However, algal biomass is also emerging as a sustainable raw material for the bioeconomy. The potential exploitation of algae is hindered by our limited knowledge of the microbial pathways-and hence the distinct biochemical functions of the enzymes involved-that convert algal polysaccharides into oligo- and monosaccharides. Understanding these processes would be essential, however, for applications such as the fermentation of algal biomass into bioethanol or other value-added compounds. Here, we describe the metabolic pathway that enables the marine flavobacterium Formosa agariphila to degrade ulvan, the main cell wall polysaccharide of bloom-forming Ulva species. The pathway involves 12 biochemically characterized carbohydrate-active enzymes, including two polysaccharide lyases, three sulfatases and seven glycoside hydrolases that sequentially break down ulvan into fermentable monosaccharides. This way, the enzymes turn a previously unexploited renewable into a valuable and ecologically sustainable bioresource. PubMed: 31285597DOI: 10.1038/s41589-019-0311-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.912 Å) |
Structure validation
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