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<StructureSection load='1y1e' size='340' side='right'caption='[[1y1e]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
<StructureSection load='1y1e' size='340' side='right'caption='[[1y1e]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1y1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1E FirstGlance]. <br>
<table><tr><td colspan='2'>[[1y1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y1f|1y1f]], [[1y1g|1y1g]], [[1y1h|1y1h]], [[1y1i|1y1i]], [[1y1j|1y1j]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1e OCA], [https://pdbe.org/1y1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1e RCSB], [https://www.ebi.ac.uk/pdbsum/1y1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1e ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1e OCA], [https://pdbe.org/1y1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1e RCSB], [https://www.ebi.ac.uk/pdbsum/1y1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1e ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN]] Defects in SUMF1 are the cause of multiple sulfatase deficiency (MSD) [MIM:[https://omim.org/entry/272200 272200]]. MSD is a clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Inheritance is autosomal recessive.<ref>PMID:12757706</ref> <ref>PMID:12757705</ref> <ref>PMID:15146462</ref> <ref>PMID:18157819</ref>
[https://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN] Defects in SUMF1 are the cause of multiple sulfatase deficiency (MSD) [MIM:[https://omim.org/entry/272200 272200]. MSD is a clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Inheritance is autosomal recessive.<ref>PMID:12757706</ref> <ref>PMID:12757705</ref> <ref>PMID:15146462</ref> <ref>PMID:18157819</ref>  
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN]] Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE.<ref>PMID:12757706</ref> <ref>PMID:15657036</ref>
[https://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN] Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE.<ref>PMID:12757706</ref> <ref>PMID:15657036</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y1e ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y1e ConSurf].
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== Publication Abstract from PubMed ==
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.
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<ref>PMID:15907468</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1y1e" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dickmanns, A]]
[[Category: Dickmanns A]]
[[Category: Ficner, R]]
[[Category: Ficner R]]
[[Category: Rudolph, M G]]
[[Category: Rudolph MG]]
[[Category: Cysteine sulfenic acid]]
[[Category: Formylglycine]]
[[Category: Multiple sulfatase deficiency]]
[[Category: Oxidoreductase]]

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