7Y4I
Crystal structure of SPINDLY in complex with GDP
Summary for 7Y4I
| Entry DOI | 10.2210/pdb7y4i/pdb |
| Descriptor | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | o-fucosyltransferase, plant protein, transferase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 203498.86 |
| Authors | |
| Primary citation | Zhu, L.,Wei, X.,Cong, J.,Zou, J.,Wan, L.,Xu, S. Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY. Nat Commun, 13:7424-7424, 2022 Cited by PubMed Abstract: Arabidopsis glycosyltransferase family 41 (GT41) protein SPINDLY (SPY) plays pleiotropic roles in plant development. Despite the amino acid sequence is similar to human O-GlcNAc transferase, Arabidopsis SPY has been identified as a novel nucleocytoplasmic protein O-fucosyltransferase. SPY-like proteins extensively exist in diverse organisms, indicating that O-fucosylation by SPY is a common way to regulate intracellular protein functions. However, the details of how SPY recognizes and glycosylates substrates are unknown. Here, we present a crystal structure of Arabidopsis SPY/GDP complex at 2.85 Å resolution. SPY adopts a head-to-tail dimer. Strikingly, the conformation of a 'catalytic SPY'/GDP/'substrate SPY' complex formed by two symmetry-related SPY dimers is captured in the crystal lattice. The structure together with mutagenesis and enzymatic data demonstrate SPY can fucosylate itself and SPY's self-fucosylation region negatively regulates its enzyme activity, reveal SPY's substrate recognition and enzyme mechanism, and provide insights into the glycan donor substrate selection in GT41 proteins. PubMed: 36456586DOI: 10.1038/s41467-022-35234-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
Download full validation report
