8PEJ
CjGH35 with a Galactosidase Activity-Based Probe
Summary for 8PEJ
| Entry DOI | 10.2210/pdb8pej/pdb |
| Descriptor | Beta-galactosidase, putative, bgl35A, SODIUM ION, (1~{S},2~{S},4~{S},5~{R})-6-(hydroxymethyl)cyclohexane-1,2,3,4,5-pentol, ... (5 entities in total) |
| Functional Keywords | beta-galactosidase, complex, activity-based probe, hydrolase |
| Biological source | Cellvibrio japonicus Ueda107 |
| Total number of polymer chains | 8 |
| Total formula weight | 500200.91 |
| Authors | Offen, W.A.,Davies, G.J. (deposition date: 2023-06-14, release date: 2023-10-04, Last modification date: 2024-10-23) |
| Primary citation | Kuo, C.L.,Su, Q.,van den Nieuwendijk, A.M.C.H.,Beenakker, T.J.M.,Offen, W.A.,Willems, L.I.,Boot, R.G.,Sarris, A.J.,Marques, A.R.A.,Codee, J.D.C.,van der Marel, G.A.,Florea, B.I.,Davies, G.J.,Overkleeft, H.S.,Aerts, J.M.F.G. The development of a broad-spectrum retaining beta-exo-galactosidase activity-based probe. Org.Biomol.Chem., 21:7813-7820, 2023 Cited by PubMed Abstract: Acid β-galactosidase (GLB1) and galactocerebrosidase (GALC) are retaining exo-β-galactosidases involved in lysosomal glycoconjugate metabolism. Deficiency of GLB1 may result in the lysosomal storage disorders GM1 gangliosidosis, Morquio B syndrome, and galactosialidosis, and deficiency of GALC may result in Krabbe disease. Activity-based protein profiling (ABPP) is a powerful technique to assess the activity of retaining glycosidases in relation to health and disease. This work describes the use of fluorescent and biotin-carrying activity-based probes (ABPs) to assess the activity of both GLB1 and GALC in cell lysates, culture media, and tissue extracts. The reported ABPs, which complement the growing list of retaining glycosidase ABPs based on configurational isomers of cyclophellitol, should assist in fundamental and clinical research on various β-galactosidases, whose inherited deficiencies cause debilitating lysosomal storage disorders. PubMed: 37724332DOI: 10.1039/d3ob01261a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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