1BHG

HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION

Summary for 1BHG

• Entry DOI: 10.2210/pdb1bhg/pdb
• Descriptor: BETA-GLUCURONIDASE, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: lysosomal enzyme, acid hydrolase, glycosidase
• Biological source: Homo sapiens (human)
• Cellular location: Lysosome: P08236
• Total number of polymer chains: 2
• Total formula weight: 144644.51

Authors

Jain, S.,Drendel, W.B. (deposition date: 1996-03-04, release date: 1997-09-17, Last modification date: 2020-07-29)

Primary citation

Jain, S.,Drendel, W.B.,Chen, Z.W.,Mathews, F.S.,Sly, W.S.,Grubb, J.H.
Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs.
Nat.Struct.Biol., 3:375-381, 1996

PubMed Abstract: The X-ray structure of the homotetrameric lysosomal acid hydrolase, human beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution. The tetramer has approximate dihedral symmetry and each promoter consists of three structural domains with topologies similar to a jelly roll barrel, an immunoglobulin constant domain and a TIM barrel respectively. Residues 179-204 form a beta-hairpin motif similar to the putative lysosomal targeting motif of cathepsin D, supporting the view that lysosomal targeting has a structural basis. The active site of the enzyme is formed from a large cleft at the interface of two monomers. Residues Glu 451 and Glu 540 are proposed to be important for catalysis. The structure establishes a framework for understanding mutations that lead to the human genetic disease mucopolysaccharidosis VII, and for using the enzyme in anti-cancer therapy.

PubMed: 8599764
DOI: 10.1038/nsb0496-375

Experimental method

X-RAY DIFFRACTION (2.53 Å)