1bhg
From Proteopedia
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[[Image:1bhg.gif|left|200px]] | [[Image:1bhg.gif|left|200px]] | ||
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'''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION''' | '''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION''' | ||
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[[Category: Drendel, W B.]] | [[Category: Drendel, W B.]] | ||
[[Category: Jain, S.]] | [[Category: Jain, S.]] | ||
- | [[Category: | + | [[Category: Acid hydrolase]] |
- | [[Category: | + | [[Category: Glycosidase]] |
- | [[Category: | + | [[Category: Lysosomal enzyme]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:31:05 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 08:31, 2 May 2008
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 Page seeded by OCA on Fri May 2 11:31:05 2008