6DEY
Aspartylglucosaminuria mutant structure and function
Summary for 6DEY
| Entry DOI | 10.2210/pdb6dey/pdb |
| Descriptor | Glycosylasparaginase, residues 38-178, Glycosylasparaginase, residues 188-331 (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) More |
| Total number of polymer chains | 4 |
| Total formula weight | 62150.96 |
| Authors | Pande, S.,Laksminarasimhan, D.,Guo, H.C. (deposition date: 2018-05-13, release date: 2018-08-01, Last modification date: 2024-03-13) |
| Primary citation | Pande, S.,Bizilj, W.,Guo, H.C. Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria. FEBS Lett., 592:2550-2561, 2018 Cited by PubMed Abstract: Aspartylglucosaminuria (AGU) is a lysosomal storage disorder caused by defects of the hydrolase glycosylasparaginase (GA). Previously, we showed that a Canadian AGU mutation disrupts an obligatory intramolecular autoprocessing with the enzyme trapped as an inactive precursor. Here, we report biochemical and structural characterizations of a model enzyme corresponding to a Finnish AGU allele, the T234I variant. Unlike the Canadian counterpart, the Finnish variant is capable of a slow autoprocessing to generate detectible hydrolyzation activity of the natural substrate of GA. We have determined a 1.6 Å-resolution structure of the Finnish AGU model and built an enzyme-substrate complex to provide a structural basis for analyzing the negative effects of the point mutation on K and k of the mature enzyme. PubMed: 29993127DOI: 10.1002/1873-3468.13190 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
Download full validation report
