1apz
From Proteopedia
(New page: 200px<br /> <applet load="1apz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1apz, resolution 2.3Å" /> '''HUMAN ASPARTYLGLUCOS...) |
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA]]. | + | 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]]. Structure known Active Sites: B and D. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846222 8846222] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846222 8846222] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Oinonen, C.]] | [[Category: Oinonen, C.]] | ||
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[[Category: glycosylasparaginase]] | [[Category: glycosylasparaginase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:03:50 2007'' |
Revision as of 11:59, 30 October 2007
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HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT
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 ... [(full description)]
About this Structure
1APZ is a [Single protein] structure of sequence from [Homo sapiens] with NAG and ASP as [ligands]. Active as [N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [3.5.1.26]. Structure known Active Sites: B and D. 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
Page seeded by OCA on Tue Oct 30 14:03:50 2007
