1y1g

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[[Image:1y1g.png|left|200px]]
 
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==Human formylglycine generating enzyme, double sulfonic acid form==
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The line below this paragraph, containing "STRUCTURE_1y1g", creates the "Structure Box" on the page.
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<StructureSection load='1y1g' size='340' side='right'caption='[[1y1g]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1y1g]] 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=1Y1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1G FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
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<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>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
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{{STRUCTURE_1y1g| PDB=1y1g | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1g OCA], [https://pdbe.org/1y1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1g RCSB], [https://www.ebi.ac.uk/pdbsum/1y1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1g ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y1/1y1g_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1y1g ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Human formylglycine generating enzyme, double sulfonic acid form===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1y1g" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15907468}}, adds the Publication Abstract to the page
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*[[Sulfatase-modifying factor|Sulfatase-modifying factor]]
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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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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15907468}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1y1g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1G OCA].
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==Reference==
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<ref group="xtra">PMID:015907468</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Dickmanns, A.]]
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[[Category: Large Structures]]
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[[Category: Ficner, R.]]
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[[Category: Dickmanns A]]
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[[Category: Rudolph, M G.]]
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[[Category: Ficner R]]
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[[Category: Cysteine sulfenic acid]]
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[[Category: Rudolph MG]]
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[[Category: Formylglycine]]
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[[Category: Multiple sulfatase deficiency]]
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[[Category: Oxidoreductase]]
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Current revision

Human formylglycine generating enzyme, double sulfonic acid form

PDB ID 1y1g

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