1apy: Difference between revisions
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|PDB= 1apy |SIZE=350|CAPTION= <scene name='initialview01'>1apy</scene>, resolution 2.0Å | |PDB= 1apy |SIZE=350|CAPTION= <scene name='initialview01'>1apy</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=B1:A+Catalytic+Residue'>B1</scene> and <scene name='pdbsite=D1:A+Catalytic+Residue'>D1</scene> | |SITE= <scene name='pdbsite=B1:A+Catalytic+Residue'>B1</scene> and <scene name='pdbsite=D1:A+Catalytic+Residue'>D1</scene> | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://www.ebi.ac.uk/pdbsum/1apy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Oinonen, C.]] | [[Category: Oinonen, C.]] | ||
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
[[Category: aspartylglucosaminidase]] | [[Category: aspartylglucosaminidase]] | ||
[[Category: glycosylasparaginase]] | [[Category: glycosylasparaginase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:12 2008'' | ||
