1fsu: Difference between revisions

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-[[Image:1fsu.gif|left|200px]]<br />
-<applet load="1fsu" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fsu, resolution 2.5&Aring;" />
-'''4-SULFATASE (HUMAN)'''<br />
-==Overview==
+==Crystal Structure of 4-Sulfatase (human)==
-BACKGROUND:. Sulfatases catalyze the hydrolysis of sulfuric acid esters, from a wide variety of substrates including glycosaminoglycans, glycolipids and steroids. There is sufficient common sequence similarity, within the class of sulfatase enzymes to indicate that they have a common, structure. Deficiencies of specific lysosomal sulfatases that are involved, in the degradation of glycosamino-glycans lead to rare inherited clinical, disorders termed mucopolysaccharidoses. In sufferers of multiple sulfatase, deficiency, all sulfatases are inactive because an essential, post-translational modification of a specific active-site cysteine residue, to oxo-alanine does not occur. Studies of this disorder have contributed, to location and characterization of the sulfatase active site. To, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9032078 (full description)]]
+<StructureSection load='1fsu' size='340' side='right'caption='[[1fsu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fsu]] 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=1FSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FSU FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALS:(3S)-3-(SULFOOXY)-L-SERINE'>ALS</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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fsu OCA], [https://pdbe.org/1fsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fsu RCSB], [https://www.ebi.ac.uk/pdbsum/1fsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fsu ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ARSB_HUMAN ARSB_HUMAN] Defects in ARSB are the cause of mucopolysaccharidosis type 6 (MPS6) [MIM:[https://omim.org/entry/253200 253200]; also known as Maroteaux-Lamy syndrome. MPS6 is an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of dermatan sulfate. Clinical features can include abnormal growth, short stature, stiff joints, skeletal malformations, corneal clouding, hepatosplenomegaly, and cardiac abnormalities. A wide variation in clinical severity is observed.<ref>PMID:1718978</ref> <ref>PMID:1550123</ref> <ref>PMID:8116615</ref> <ref>PMID:8125475</ref> <ref>PMID:8541342</ref> <ref>PMID:8651289</ref> <ref>PMID:10036316</ref> <ref>PMID:10738004</ref> <ref>PMID:11802522</ref> <ref>PMID:14974081</ref>   Arylsulfatase B activity is defective in multiple sulfatase deficiency (MSD) [MIM:[https://omim.org/entry/272200 272200]. 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. Note=Arylsulfatase B activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSB at residue Cys-91 that is not converted to 3-oxoalanine.<ref>PMID:7628016</ref> <ref>PMID:15146462</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ARSB_HUMAN ARSB_HUMAN]
+== 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/fs/1fsu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1fsu ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FSU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.12 3.1.6.12]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FSU OCA]].
+*[[Sulfatase 3D structures|Sulfatase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Structure of a human lysosomal sulfatase., Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM, Structure. 1997 Feb 15;5(2):277-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9032078 9032078]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bond, C.]]
+[[Category: Bond C]]
-[[Category: Guss, M.]]
+[[Category: Guss M]]
-[[Category: CA]]
-[[Category: CL]]
-[[Category: glycoprotein]]
-[[Category: glycosaminoglycan degradation]]
-[[Category: hydrolase]]
-[[Category: lysosome]]
-[[Category: signal]]
-[[Category: sulfatase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:18:41 2007''