1y1g

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[[Image:1y1g.gif|left|200px]]
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{{Seed}}
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[[Image:1y1g.png|left|200px]]
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{{STRUCTURE_1y1g| PDB=1y1g | SCENE= }}
{{STRUCTURE_1y1g| PDB=1y1g | SCENE= }}
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'''human formylglycine generating enzyme, double sulfonic acid form'''
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===human formylglycine generating enzyme, double sulfonic acid form===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15907468 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15907468}}
==About this Structure==
==About this Structure==
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[[Category: Formylglycine]]
[[Category: Formylglycine]]
[[Category: Multiple sulfatase deficiency]]
[[Category: Multiple sulfatase deficiency]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:07:07 2008''

Revision as of 10:07, 28 July 2008

Image:1y1g.png

Template:STRUCTURE 1y1g

human formylglycine generating enzyme, double sulfonic acid form

Template:ABSTRACT PUBMED 15907468

About this Structure

1Y1G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme., Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, von Figura K, Ficner R, Rudolph MG, Cell. 2005 May 20;121(4):541-52. PMID:15907468

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