1bhg
From Proteopedia
(New page: 200px<br /> <applet load="1bhg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhg, resolution 2.53Å" /> '''HUMAN BETA-GLUCURON...) |
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| - | [[Image:1bhg.gif|left|200px]]<br /> | + | [[Image:1bhg.gif|left|200px]]<br /><applet load="1bhg" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1bhg, resolution 2.53Å" /> | caption="1bhg, resolution 2.53Å" /> | ||
'''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION'''<br /> | '''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray structure of the homotetrameric lysosomal acid hydrolase, human | + | 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== | ==Disease== | ||
| - | Known disease associated with this structure: Mucopolysaccharidosis VII OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id= | + | Known disease associated with this structure: Mucopolysaccharidosis VII OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611499 611499]] |
==About this Structure== | ==About this Structure== | ||
| - | 1BHG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http:// | + | 1BHG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Drendel, W | + | [[Category: Drendel, W B.]] |
[[Category: Jain, S.]] | [[Category: Jain, S.]] | ||
[[Category: acid hydrolase]] | [[Category: acid hydrolase]] | ||
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[[Category: lysosomal enzyme]] | [[Category: lysosomal enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:23 2008'' |
Revision as of 09:55, 21 February 2008
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HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION
Contents |
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. Active as Beta-glucuronidase, with EC number 3.2.1.31 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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