1y4j
From Proteopedia
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|PDB= 1y4j |SIZE=350|CAPTION= <scene name='initialview01'>1y4j</scene>, resolution 1.864Å | |PDB= 1y4j |SIZE=350|CAPTION= <scene name='initialview01'>1y4j</scene>, resolution 1.864Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SUMF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SUMF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1y1e|1Y1E]], [[1y1f|1Y1F]], [[1y1g|1Y1G]], [[1y1h|1Y1H]], [[1y1i|1Y1I]], [[1y1j|1Y1J]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4j OCA], [http://www.ebi.ac.uk/pdbsum/1y4j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y4j RCSB]</span> | ||
}} | }} | ||
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[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
[[Category: Rudolph, M G.]] | [[Category: Rudolph, M G.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MPD]] | ||
[[Category: duf323]] | [[Category: duf323]] | ||
[[Category: formylglycine]] | [[Category: formylglycine]] | ||
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[[Category: sulfatase]] | [[Category: sulfatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:58:41 2008'' |
Revision as of 21:58, 30 March 2008
| |||||||
| , resolution 1.864Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | SUMF2 (Homo sapiens) | ||||||
| Related: | 1Y1E, 1Y1F, 1Y1G, 1Y1H, 1Y1I, 1Y1J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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