2IXB

Crystal structure of N-ACETYLGALACTOSAMINIDASE in complex with GalNAC

Summary for 2IXB

• Entry DOI: 10.2210/pdb2ixb/pdb
• Related: 2IXA
• Descriptor: ALPHA-N-ACETYLGALACTOSAMINIDASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, 2-acetamido-2-deoxy-alpha-D-galactopyranose, ... (6 entities in total)
• Functional Keywords: n-acetylgalactosaminidase, nad, a-eco conversion, hydrolase
• Biological source: FLAVOBACTERIUM MENINGOSEPTICUM
• Total number of polymer chains: 1
• Total formula weight: 51520.90

Authors

Sulzenbacher, G.,Liu, Q.P.,Bourne, Y.,Henrissat, B.,Clausen, H. (deposition date: 2006-07-07, release date: 2007-04-10, Last modification date: 2023-12-13)

Primary citation

Liu, Q.P.,Sulzenbacher, G.,Yuan, H.,Bennett, E.P.,Pietz, G.,Saunders, K.,Spence, J.,Nudelman, E.,Levery, S.B.,White, T.,Neveu, J.M.,Lane, W.S.,Bourne, Y.,Olsson, M.L.,Henrissat, B.,Clausen, H.
Bacterial Glycosidases for the Production of Universal Red Blood Cells.
Nat.Biotechnol., 25:454-, 2007

PubMed Abstract: Enzymatic removal of blood group ABO antigens to develop universal red blood cells (RBCs) was a pioneering vision originally proposed more than 25 years ago. Although the feasibility of this approach was demonstrated in clinical trials for group B RBCs, a major obstacle in translating this technology to clinical practice has been the lack of efficient glycosidase enzymes. Here we report two bacterial glycosidase gene families that provide enzymes capable of efficient removal of A and B antigens at neutral pH with low consumption of recombinant enzymes. The crystal structure of a member of the alpha-N-acetylgalactosaminidase family reveals an unusual catalytic mechanism involving NAD+. The enzymatic conversion processes we describe hold promise for achieving the goal of producing universal RBCs, which would improve the blood supply while enhancing the safety of clinical transfusions.

PubMed: 17401360
DOI: 10.1038/NBT1298

Experimental method

X-RAY DIFFRACTION (2.4 Å)