8xfr | pdb_00008xfr

Structure of the alginate epimerase/lyase complexed with tetra-mannuronic acid

spinqualitylabelsall models 8xfr, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xfr is a 1 chain structure with sequence from Azotobacter chroococcum NCIMB 8003. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ACT, BEM, CA, MLY, PEG, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0C4WKK2_9GAMM Publication Abstract from PubMed Among the epimerases specific to alginate, some of them in Azotobacter genera convert beta-d-mannuronic acid to alpha-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. Structural basis for the minimal bifunctional alginate epimerase AlgE3 from Azotobacter chroococcum.,Fujiwara T, Mano E, Nango E FEBS Lett. 2024 Apr 22. doi: 10.1002/1873-3468.14886. PMID:38649293 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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