9I4F
Blood Type B-converting alpha-1,3-galactosidase PpaGal from Pedobacter panaciterrae in its apo form
This is a non-PDB format compatible entry.
Summary for 9I4F
Entry DOI | 10.2210/pdb9i4f/pdb |
Descriptor | Alpha-1,3-galactosidase PpaGal, 1,2-ETHANEDIOL (3 entities in total) |
Functional Keywords | alpha-1, 3-galactopyranosidase, galactosidase, d-galactose, blood conversion, b-antigen removal, beta-helix, beta-barrel, hydrolase |
Biological source | Pedobacter panaciterrae |
Total number of polymer chains | 4 |
Total formula weight | 263497.26 |
Authors | Schmoeker, O.,Moeller, C.,Terholsen, H.,Girbardt, B.,Palm, G.J.,Hoppen, J.,Lammers, M.,Bornscheuer, U.T. (deposition date: 2025-01-24, release date: 2025-03-12, Last modification date: 2025-04-30) |
Primary citation | Moller, C.,Terholsen, H.,Schmoker, O.,Le, T.L.A.,Wesche, J.,Schmiade, P.,Eppendorfer, E.,Rimkus, N.,Girbardt, B.,Bottcher, D.,Palm, G.J.,Hoppen, J.,Lammers, M.,Greinacher, A.,Aurich, K.,Bornscheuer, U.T. Identification and Protein Engineering of Galactosidases for the Conversion of Blood Type B to Blood Type O. Chembiochem, 26:e202500072-e202500072, 2025 Cited by PubMed Abstract: The supply of blood products such as red blood cells poses a challenge due to rising demand and declining donor numbers. Careful matching of blood products of different types is required. Only type O of the blood types A, B, AB and O can be received by any patient without transfusion incompatibilities. Therefore, O-type blood can be considered "universal blood" and is especially needed in emergency situations. In this study, we focused on the conversion of the B antigen by enzymatic deglycosylation to generate the H antigen determining O-type blood. For this, we characterized several previously unstudied α-1,3-galactosidases belonging to the GH110 family. Our findings revealed that the α-1,3-galactosidase from Pedobacter panaciterrae (PpaGal) exhibits superior efficiency compared to previously described galactosidases. We further increased the activity of PpaGal by 2.5-fold using site-directed mutagenesis. Moreover, we solved two crystal structures of PpaGal, one in the apo-state and another in complex with d-galactose. The combination of our mutagenesis study with the solved crystal structures provides valuable information to guide further optimization of PpaGal or other B antigen converting enzymes paving the way for the easier production of universal blood from B-type blood. PubMed: 40013737DOI: 10.1002/cbic.202500072 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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