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1y4j

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[[Image:1y4j.gif|left|200px]]<br /><applet load="1y4j" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y4j.gif|left|200px]]
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caption="1y4j, resolution 1.864&Aring;" />
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'''Crystal structure of the paralogue of the human formylglycine generating enzyme'''<br />
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{{Structure
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|PDB= 1y4j |SIZE=350|CAPTION= <scene name='initialview01'>1y4j</scene>, resolution 1.864&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY=
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|GENE= SUMF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of the paralogue of the human formylglycine generating enzyme'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y4J 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 <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4J OCA].
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1Y4J is a [[Single protein]] 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=1Y4J OCA].
==Reference==
==Reference==
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Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme., Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R, J Biol Chem. 2005 Apr 15;280(15):15180-7. Epub 2005 Feb 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15687489 15687489]
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Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme., Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R, J Biol Chem. 2005 Apr 15;280(15):15180-7. Epub 2005 Feb 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15687489 15687489]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: homodimer]]
[[Category: homodimer]]
[[Category: multiple sulfatase deficiency]]
[[Category: multiple sulfatase deficiency]]
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[[Category: sulfatases]]
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[[Category: sulfatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:18:21 2008''

Revision as of 13:18, 20 March 2008


PDB ID 1y4j

Drag the structure with the mouse to rotate
, resolution 1.864Å
Ligands: and
Gene: SUMF2 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the paralogue of the human formylglycine generating enzyme


Overview

In eukaryotes, sulfate esters are degraded by sulfatases, which possess a unique Calpha-formylglycine residue in their active site. The defect in post-translational formation of the Calpha-formylglycine residue causes a severe lysosomal storage disorder in humans. Recently, FGE (formylglycine-generating enzyme) has been identified as the protein required for this specific modification. Using sequence comparisons, a protein homologous to FGE was found and denoted pFGE (paralog of FGE). pFGE binds a sulfatase-derived peptide bearing the FGE recognition motif, but it lacks formylglycine-generating activity. Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure. We have crystallized the glycosylated human pFGE and determined its crystal structure at a resolution of 1.86 A. The structure reveals a novel fold, which we denote the FGE fold and which therefore serves as a paradigm for the DUF323 domain. It is characterized by an asymmetric partitioning of secondary structure elements and is stabilized by two calcium cations. A deep cleft on the surface of pFGE most likely represents the sulfatase polypeptide binding site. The asymmetric unit of the pFGE crystal contains a homodimer. The putative peptide binding site is buried between the monomers, indicating a biological significance of the dimer. The structure suggests the capability of pFGE to form a heterodimer with FGE.

About this Structure

1Y4J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme., Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R, J Biol Chem. 2005 Apr 15;280(15):15180-7. Epub 2005 Feb 1. PMID:15687489

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