1apy: Difference between revisions
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[[Image:1apy.gif|left|200px]]<br /><applet load="1apy" size=" | [[Image:1apy.gif|left|200px]]<br /><applet load="1apy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1apy, resolution 2.0Å" /> | caption="1apy, resolution 2.0Å" /> | ||
'''HUMAN ASPARTYLGLUCOSAMINIDASE'''<br /> | '''HUMAN ASPARTYLGLUCOSAMINIDASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1APY 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=B1:A Catalytic Residue'>B1</scene> and <scene name='pdbsite=D1:A Catalytic Residue'>D1</scene>. Full crystallographic information is available from [http:// | 1APY 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=B1:A+Catalytic+Residue'>B1</scene> and <scene name='pdbsite=D1:A+Catalytic+Residue'>D1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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Revision as of 10:31, 3 February 2008
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HUMAN ASPARTYLGLUCOSAMINIDASE
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Aspartylglucosaminuria OMIM:[208400]
About this StructureAbout this Structure
1APY is a Single protein structure of sequence from Homo sapiens with as ligand. 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.
ReferenceReference
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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