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8XFQ

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

This is a non-PDB format compatible entry.
Summary for 8XFQ
Entry DOI10.2210/pdb8xfq/pdb
Related8JA4 8JA6 8JAZ
Descriptormannuronan 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 Keywordssubstrate, complex, epimerase, isomerase
Biological sourceAzotobacter chroococcum NCIMB 8003
Total number of polymer chains1
Total formula weight53114.78
Authors
Fujiwara, T. (deposition date: 2023-12-14, release date: 2024-05-15, 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 (2.25 Å)
Structure validation

227344

數據於2024-11-13公開中

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