5Z1X
Crystal Structure of Laccase from Cerrena sp. RSD1
Summary for 5Z1X
| Entry DOI | 10.2210/pdb5z1x/pdb |
| Descriptor | Laccase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | laccase, copper-dependent enzyme, oxidoreductase |
| Biological source | Cerrena sp. RSD1 |
| Total number of polymer chains | 2 |
| Total formula weight | 108746.17 |
| Authors | Lee, C.C.,Wu, M.H.,Ho, T.H.,Wang, A.H.J. (deposition date: 2017-12-28, release date: 2018-09-05, Last modification date: 2024-11-06) |
| Primary citation | Wu, M.H.,Lee, C.C.,Hsiao, A.S.,Yu, S.M.,Wang, A.H.J.,Ho, T.D. Kinetic analysis and structural studies of a high-efficiency laccase fromCerrenasp. RSD1. FEBS Open Bio, 8:1230-1246, 2018 Cited by PubMed Abstract: A high-efficiency laccase, DLac, was isolated from sp. RSD1. The kinetic studies indicate that DLac is a diffusion-limited enzyme. The crystal structure of DLac was determined to atomic resolution, and its overall structure shares high homology to monomeric laccases, but displays unique substrate-binding loops from those in other laccases. The substrate-binding residues with small side chain and the short substrate-binding loop IV broaden the substrate-binding cavity and may facilitate large substrate diffusion. Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468. The -glycans stabilize the substrate-binding loops and the protein structure, and the first -acetylglucosamine is crucial for the catalytic efficiency. Additionally, a fivefold increase in protein yield is achieved via the submerged culture method for industrial applications. PubMed: 30087829DOI: 10.1002/2211-5463.12459 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.38 Å) |
Structure validation
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