2hi8

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{{STRUCTURE_2hi8| PDB=2hi8 | SCENE= }}
 
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===human formylglycine generating enzyme, C336S mutant, bromide co-crystallization===
 
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{{ABSTRACT_PUBMED_17452787}}
 
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==Disease==
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==human formylglycine generating enzyme, C336S mutant, bromide co-crystallization==
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[[http://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN]] Defects in SUMF1 are the cause of multiple sulfatase deficiency (MSD) [MIM:[http://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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<StructureSection load='2hi8' size='340' side='right'caption='[[2hi8]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hi8]] is a 2 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=2HI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HI8 FirstGlance]. <br>
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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]] 1.64&#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=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=2hi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hi8 OCA], [https://pdbe.org/2hi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hi8 RCSB], [https://www.ebi.ac.uk/pdbsum/2hi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hi8 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/hi/2hi8_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=2hi8 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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The catalytic residue in sulfatases is a unique formylglycine that is post-translationally generated by oxidation of a cysteine or serine precursor. Molecular oxygen oxidizes the cysteine precursor in eukaryotic sulfatases, a reaction that is catalysed by the formylglycine-generating enzyme FGE. Previously, FGE was crystallized in complex with a chloride ion which, based on its similar polarizability and hydrophobicity, indicates the site of molecular oxygen binding. Here, two structures of FGE in complex with bromide and iodide were determined in order to further delineate the volume and stereochemical restraints of the oxygen-binding site for potential reaction intermediates. Anomalous difference density maps unambiguously assigned the nature of the halide ions. Unexpectedly, data collected at a wavelength of 1.54 A from the iodide-containing crystal and data collected at a wavelength of 0.8 A from a bromide-containing crystal were sufficient for SIRAS phasing.
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==Function==
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Probing the oxygen-binding site of the human formylglycine-generating enzyme using halide ions.,Roeser D, Schmidt B, Preusser-Kunze A, Rudolph MG Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):621-7. Epub 2007, Apr 21. PMID:17452787<ref>PMID:17452787</ref>
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[[http://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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2hi8]] is a 2 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=2HI8 OCA].
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</div>
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<div class="pdbe-citations 2hi8" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:017452787</ref><references group="xtra"/><references/>
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*[[Sulfatase-modifying factor|Sulfatase-modifying factor]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Roeser, D.]]
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[[Category: Large Structures]]
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[[Category: Rudolph, M G.]]
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[[Category: Roeser D]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Rudolph MG]]
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[[Category: Formylglycin generation]]
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[[Category: Hydrolase activator]]
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[[Category: Post-translational modification]]
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[[Category: Protein binding]]
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[[Category: Sulfatase]]
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Current revision

human formylglycine generating enzyme, C336S mutant, bromide co-crystallization

PDB ID 2hi8

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