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7NCZ

Crystal structure of Paradendryphiella salina PL7A alginate lyase mutant Y223F in complex with hexa-mannuronic acid

Summary for 7NCZ
Entry DOI10.2210/pdb7ncz/pdb
Related6YWF
DescriptorAlginate lyase (PL7), 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-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
Functional Keywordscomplex, beta jelly roll, mutant, alginate lyase, lyase
Biological sourceParadendryphiella salina
Total number of polymer chains1
Total formula weight26912.84
Authors
Fredslund, F.,Welner, D.H.,Wilkens, C. (deposition date: 2021-01-29, release date: 2022-03-02, Last modification date: 2025-07-02)
Primary citationRivas-Fernandez, J.P.,Vuillemin, M.,Pilgaard, B.,Klau, L.J.,Fredslund, F.,Lund-Hanssen, C.,Welner, D.H.,Meyer, A.S.,Morth, J.P.,Meilleur, F.,Aachmann, F.L.,Rovira, C.,Wilkens, C.
Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation.
Nat Commun, 16:2670-2670, 2025
Cited by
PubMed Abstract: Alginate lyases (ALs) catalyze the depolymerization of brown macroalgae alginates, widely used naturally occurring polysaccharides. Their molecular reaction mechanism remains elusive due to the lack of catalytically competent Michaelis-Menten-like complex structures. Here, we provide structural snapshots and dissect the mechanism of mannuronan-specific ALs from family 7 polysaccharide lyases (PL7), employing time-resolved NMR, X-ray, neutron crystallography, and QM/MM simulations. We reveal the protonation state of critical active site residues, enabling atomic-level analysis of the reaction coordinate. Our approach reveals an endolytic and asynchronous syn β-elimination reaction, with Tyr serving as both Brønsted base and acid, involving a carbanion-type transition state. This study not only reconciles previous structural and kinetic discrepancies, but also establishes a comprehensive PL reaction mechanism which is most likely applicable across all enzymes of the PL7 family as well as other PL families.
PubMed: 40102416
DOI: 10.1038/s41467-025-56754-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.64 Å)
Structure validation

238582

数据于2025-07-09公开中

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