1apz
From Proteopedia
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| - | [[Image:1apz.gif|left|200px]]<br /><applet load="1apz" size=" | + | [[Image:1apz.gif|left|200px]]<br /><applet load="1apz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1apz, resolution 2.3Å" /> | caption="1apz, resolution 2.3Å" /> | ||
'''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT'''<br /> | '''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1APZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and ASP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] Known structural/functional Sites: <scene name='pdbsite=B:A Catalytic Residue'>B</scene> and <scene name='pdbsite=D:A Catalytic Residue'>D</scene>. Full crystallographic information is available from [http:// | + | 1APZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] Known structural/functional Sites: <scene name='pdbsite=B:A+Catalytic+Residue'>B</scene> and <scene name='pdbsite=D:A+Catalytic+Residue'>D</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glycosylasparaginase]] | [[Category: glycosylasparaginase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:31:15 2008'' |
Revision as of 07:31, 3 February 2008
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HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT
Contents |
Overview
The high resolution crystal structure of human lysosomal, aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme, is synthesized as a single polypeptide precursor, which is immediately, post-translationally cleaved into alpha- and beta-subunits. Two alpha- and, beta-chains are found to pack together forming the final heterotetrameric, structure. The catalytically essential residue, the N-terminal threonine, of the beta-chain is situated in the deep pocket of the funnel-shaped, active site. On the basis of the structure of the enzyme-product complex, we present a catalytic mechanism for this lysosomal enzyme with an, exceptionally high pH optimum. The three-dimensional structure also allows, the prediction of the structural consequences of human mutations resulting, in aspartylglucosaminuria (AGU), a lysosomal storage disease.
Disease
Known disease associated with this structure: Aspartylglucosaminuria OMIM:[208400]
About this Structure
1APZ is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of human lysosomal aspartylglucosaminidase., Oinonen C, Tikkanen R, Rouvinen J, Peltonen L, Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222
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