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8JA4

Structure of the alginate epimerase/lyase

This is a non-PDB format compatible entry.
Summary for 8JA4
Entry DOI10.2210/pdb8ja4/pdb
Descriptormannuronan 5-epimerase, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordsbifunctional epimerase/lyase, isomerase
Biological sourceAzotobacter chroococcum NCIMB 8003
Total number of polymer chains1
Total formula weight53543.58
Authors
Fujiwara, T. (deposition date: 2023-05-05, release date: 2024-05-08, Last modification date: 2024-06-26)
Primary citationFujiwara, 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: 38649293
DOI: 10.1002/1873-3468.14886
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.04 Å)
Structure validation

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