1bhg | pdb_00001bhg
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| 1bhg, resolution 2.53Å | |||||||||||||
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| Ligands: | BMA, MAN, NAG | ||||||||||||
| Gene: | HUMAN PLACENTAL GUS GENE CDNA (Homo sapiens) | ||||||||||||
| Activity: | Beta-glucuronidase, with EC number 3.2.1.31 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION
Overview
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.
About this Structure
1BHG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs., Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH, Nat Struct Biol. 1996 Apr;3(4):375-81. PMID:8599764
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