8k2i | pdb_00008k2i

Crystal structure of Group 2 Oligosaccharide/Monosaccharide-releasing beta-N-acetylhexosaminidase NgaAt from Arabidopsis thaliana in complex with GlcNAc-thiazoline

spinqualitylabelsall models 8k2i, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8k2i is a 2 chain structure with sequence from Arabidopsis thaliana x Arabidopsis lyrata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CL, NGT, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7Y231_ARATH Publication Abstract from PubMed beta-N-Acetylgalactosamine-containing glycans play essential roles in several biological processes, including cell adhesion, signal transduction, and immune responses. beta-N-Acetylgalactosaminidases hydrolyze beta-N-acetylgalactosamine linkages of various glycoconjugates. However, their biological significance remains ambiguous, primarily because only one type of enzyme, exo-beta-N-acetylgalactosaminidases that specifically act on beta-N-acetylgalactosamine residues, has been documented to date. In this study, we identify four groups distributed among all three domains of life and characterize eight beta-N-acetylgalactosaminidases and beta-N-acetylhexosaminidase through sequence-based screening of deep-sea metagenomes and subsequent searching of public protein databases. Despite low sequence similarity, the crystal structures of these enzymes demonstrate that all enzymes share a prototype structure and have diversified their substrate specificities (oligosaccharide-releasing, oligosaccharide/monosaccharide-releasing, and monosaccharide-releasing) through the accumulation of mutations and insertional amino acid sequences. The diverse beta-N-acetylgalactosaminidases reported in this study could facilitate the comprehension of their structures and functions and present evolutionary pathways for expanding their substrate specificity. Genetic and functional diversity of beta-N-acetylgalactosamine-targeting glycosidases expanded by deep-sea metagenome analysis.,Sumida T, Hiraoka S, Usui K, Ishiwata A, Sengoku T, Stubbs KA, Tanaka K, Deguchi S, Fushinobu S, Nunoura T Nat Commun. 2024 May 10;15(1):3543. doi: 10.1038/s41467-024-47653-2. PMID:38730244 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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