1bhg: Difference between revisions
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'''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION''' | {{Structure | ||
|PDB= 1bhg |SIZE=350|CAPTION= <scene name='initialview01'>1bhg</scene>, resolution 2.53Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-glucuronidase Beta-glucuronidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.31 3.2.1.31] | |||
|GENE= HUMAN PLACENTAL GUS GENE CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BHG is a [ | 1BHG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8599764 8599764] | ||
[[Category: Beta-glucuronidase]] | [[Category: Beta-glucuronidase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: lysosomal enzyme]] | [[Category: lysosomal enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:11:04 2008'' | ||
Revision as of 08:11, 20 March 2008
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| 1bhg, resolution 2.53Å | |||||||||||||
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| Gene: | HUMAN PLACENTAL GUS GENE CDNA (Homo sapiens) | ||||||||||||
| Activity: | Beta-glucuronidase, with EC number 3.2.1.31 | ||||||||||||
| 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.
Disease
Known disease associated with this structure: Mucopolysaccharidosis VII OMIM:[611499]
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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