8JQF
Structure of CmCBDA in complex with Ni2+ and Glycerol
Summary for 8JQF
| Entry DOI | 10.2210/pdb8jqf/pdb |
| Descriptor | YdjC family protein, GLYCEROL, NICKEL (II) ION, ... (5 entities in total) |
| Functional Keywords | cmcbda, n-acetylglucosamine deacetylase, mentalloenzyme, enzyme engineering, hydrolase |
| Biological source | Cyclobacterium marinum |
| Total number of polymer chains | 2 |
| Total formula weight | 71162.07 |
| Authors | |
| Primary citation | Hu, S.,Xu, L.,Xie, C.,Hong, J. Structural Insights into the Catalytic Activity of Cyclobacterium marinum N -Acetylglucosamine Deacetylase. J.Agric.Food Chem., 72:783-793, 2024 Cited by PubMed Abstract: -Acetylglucosamine deacetylase from (CmCBDA) is a highly effective and selective biocatalyst for the production of d-glucosamine (GlcN) from -acetylglucosamine (GlcNAc). However, the underlying catalytic mechanism remains elusive. Here, we show that CmCBDA is a metalloenzyme with a preference for Ni over Mn. Crystal structures of CmCBDA in complex with Ni and Mn revealed slight remodeling of the CmCBDA active site by the metal ions. We also demonstrate that CmCBDA exists as a mixture of homodimers and monomers in solution, and dimerization is indispensable for catalytic activity. A mutagenesis analysis also indicated that the active site residues Asp22, His72, and His143 as well as the residues involved in dimerization, Pro52, Trp53, and Tyr55, are essential for catalytic activity. Furthermore, a mutation on the protein surface, Lys219Glu, resulted in a 2.3-fold improvement in the deacetylation activity toward GlcNAc. Mechanistic insights obtained here may facilitate the development of CmCBDA variants with higher activities. PubMed: 38141024DOI: 10.1021/acs.jafc.3c06146 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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