1y4j
From Proteopedia
(New page: 200px<br /> <applet load="1y4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4j, resolution 1.864Å" /> '''Crystal structure ...) |
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| - | [[Image:1y4j.gif|left|200px]]<br /> | + | [[Image:1y4j.gif|left|200px]]<br /><applet load="1y4j" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1y4j, resolution 1.864Å" /> | caption="1y4j, resolution 1.864Å" /> | ||
'''Crystal structure of the paralogue of the human formylglycine generating enzyme'''<br /> | '''Crystal structure of the paralogue of the human formylglycine generating enzyme'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In eukaryotes, sulfate esters are degraded by sulfatases, which possess a | + | 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== | ==About this Structure== | ||
| - | 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 CA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Dickmanns, A.]] | [[Category: Dickmanns, A.]] | ||
[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M G.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
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[[Category: sulfatases]] | [[Category: sulfatases]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:48 2008'' |
Revision as of 14:01, 21 February 2008
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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 with and as ligands. 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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