2hib: Difference between revisions

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-{{Seed}}
-[[Image:2hib.png|left|200px]]
-<!--
+==human formylglycine generating enzyme, C336S mutant, iodide co-crystallization==
-The line below this paragraph, containing "STRUCTURE_2hib", creates the "Structure Box" on the page.
+<StructureSection load='2hib' size='340' side='right'caption='[[2hib]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2hib]] 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=2HIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_2hib|  PDB=2hib  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hib OCA], [https://pdbe.org/2hib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hib RCSB], [https://www.ebi.ac.uk/pdbsum/2hib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hib ProSAT]</span></td></tr>
+</table>
+== 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>
+== 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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/2hib_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2hib ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===human formylglycine generating enzyme, C336S mutant, iodide co-crystallization===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2hib" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-HIB is a 1 chain structure of 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=2HIB OCA].
+*[[Sulfatase-modifying factor|Sulfatase-modifying factor]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Roeser, D.]]
+[[Category: Large Structures]]
-[[Category: Rudolph, M G.]]
+[[Category: Roeser D]]
-[[Category: Endoplasmic reticulum]]
+[[Category: Rudolph MG]]
-[[Category: Formylglycine]]
-[[Category: Hydrolase activator]]
-[[Category: Post-translational modification]]
-[[Category: Protein binding]]
-[[Category: Sulfatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:27:28 2009''