8XFQ
Structure of the alginate epimerase/lyase complexed with penta-mannuronic acid
This is a non-PDB format compatible entry.
Summary for 8XFQ
| Entry DOI | 10.2210/pdb8xfq/pdb |
| Related | 8JA4 8JA6 8JAZ |
| Descriptor | mannuronan 5-epimerase, beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | substrate, complex, epimerase, isomerase |
| Biological source | Azotobacter chroococcum NCIMB 8003 |
| Total number of polymer chains | 1 |
| Total formula weight | 53114.78 |
| Authors | Fujiwara, T. (deposition date: 2023-12-14, release date: 2024-05-15, Last modification date: 2024-06-26) |
| Primary citation | Fujiwara, T.,Mano, E.,Nango, E. Structural basis for the minimal bifunctional alginate epimerase AlgE3 from Azotobacter chroococcum. Febs Lett., 598:1422-1437, 2024 Cited by PubMed Abstract: Among the epimerases specific to alginate, some of them in Azotobacter genera convert β-d-mannuronic acid to α-l-guluronic acid but also have lyase activity to degrade alginate. The remarkable characteristics of these epimerases make it a promising enzyme for tailoring alginates to meet specific demands. Here, we determined the structure of the bifunctional mannuronan C-5 epimerase AlgE3 from Azotobacter chroococcum (AcAlgE3) in complex with several mannuronic acid oligomers as well as in apo form, which allowed us to elucidate the binding manner of each mannuronic acid oligomer, and the structural plasticity, which is dependent on calcium ions. Moreover, a comprehensive analysis of the lyase activity profiles of AcAlgE3 combined with structural characteristics explained the preference for different chain length oligomers. PubMed: 38649293DOI: 10.1002/1873-3468.14886 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
Download full validation report
