1KTC

The Structure of alpha-N-Acetylgalactosaminidase

Summary for 1KTC

• Entry DOI: 10.2210/pdb1ktc/pdb
• Related: 1KTB
• Descriptor: alpha-N-acetylgalactosaminidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: glycoprotein, (beta/alpha)8 barrel, protein-ligand complex, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 48194.50

Authors

Garman, S.C.,Hannick, L.,Zhu, A.,Garboczi, D.N. (deposition date: 2002-01-15, release date: 2002-03-15, Last modification date: 2024-10-30)

Primary citation

Garman, S.C.,Hannick, L.,Zhu, A.,Garboczi, D.N.
The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases.
Structure, 10:425-434, 2002

PubMed Abstract: In the lysosome, glycosidases degrade glycolipids, glycoproteins, and oligosaccharides. Mutations in glycosidases cause disorders characterized by the deposition of undegraded carbohydrates. Schindler and Fabry diseases are caused by the incomplete degradation of carbohydrates with terminal alpha-N-acetylgalactosamine and alpha-galactose, respectively. Here we present the X-ray structure of alpha-N-acetylgalactosaminidase (alpha-NAGAL), the glycosidase that removes alpha-N-acetylgalactosamine, and the structure with bound ligand. The active site residues of alpha-NAGAL are conserved in the closely related enzyme a-galactosidase A (alpha-GAL). The structure demonstrates the catalytic mechanisms of both enzymes and reveals the structural basis of mutations causing Schindler and Fabry diseases. As alpha-NAGAL and alpha-GAL produce type O "universal donor" blood from type A and type B blood, the alpha-NAGAL structure will aid in the engineering of improved enzymes for blood conversion.

PubMed: 12005440
DOI: 10.1016/S0969-2126(02)00726-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)