4U6B
Zg3597, a family 117 glycoside hydrolase, produced by the marine bacterium Zobellia galactanivorans
Summary for 4U6B
| Entry DOI | 10.2210/pdb4u6b/pdb |
| Related | 3P2N 3R4Y 4AK5 |
| Descriptor | Conserved hypothetical lipoprotein, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (7 entities in total) |
| Functional Keywords | gh117, hydrolase |
| Biological source | Zobellia galactanivorans |
| Total number of polymer chains | 4 |
| Total formula weight | 196270.40 |
| Authors | Ficko-Blean, E. (deposition date: 2014-07-28, release date: 2015-02-11, Last modification date: 2023-12-20) |
| Primary citation | Ficko-Blean, E.,Duffieux, D.,Rebuffet, E.,Larocque, R.,Groisillier, A.,Michel, G.,Czjzek, M. Biochemical and structural investigation of two paralogous glycoside hydrolases from Zobellia galactanivorans: novel insights into the evolution, dimerization plasticity and catalytic mechanism of the GH117 family. Acta Crystallogr.,Sect.D, 71:209-223, 2015 Cited by PubMed Abstract: The family 117 glycoside hydrolase (GH117) enzymes have exo-α-1,3-(3,6-anhydro)-L-galactosidase activity, removing terminal nonreducing α-1,3-linked 3,6-anhydro-L-galactose residues from their red algal neoagarose substrate. These enzymes have previously been phylogenetically divided into clades, and only the clade A enzymes have been experimentally studied to date. The investigation of two GH117 enzymes, Zg3615 and Zg3597, produced by the marine bacterium Zobellia galactanivorans reveals structural, biochemical and further phylogenetic diversity between clades. A product complex with the unusual β-3,6-anhydro-L-galactose residue sheds light on the inverting catalytic mechanism of the GH117 enzymes as well as the structure of this unique sugar produced by hydrolysis of the agarophyte red algal cell wall. PubMed: 25664732DOI: 10.1107/S1399004714025024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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