1y1j: Difference between revisions
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|PDB= 1y1j |SIZE=350|CAPTION= <scene name='initialview01'>1y1j</scene>, resolution 1.55Å | |PDB= 1y1j |SIZE=350|CAPTION= <scene name='initialview01'>1y1j</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1y1e|1Y1E]], [[1y1f|1Y1F]], [[1y1g|1Y1G]], [[1y1h|1Y1H]], [[1y1i|1Y1I]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1j OCA], [http://www.ebi.ac.uk/pdbsum/1y1j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y1j RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate. | Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
[[Category: Rudolph, M G.]] | [[Category: Rudolph, M G.]] | ||
[[Category: cysteine sulfenic acid]] | [[Category: cysteine sulfenic acid]] | ||
[[Category: formylglycine]] | [[Category: formylglycine]] | ||
[[Category: multiple sulfatase deficiency]] | [[Category: multiple sulfatase deficiency]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:57:36 2008'' | ||