1y4j: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1y4j.gif|left|200px]] | [[Image:1y4j.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1y4j", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1y4j| PDB=1y4j | SCENE= }} | |||
}} | |||
'''Crystal structure of the paralogue of the human formylglycine generating enzyme''' | '''Crystal structure of the paralogue of the human formylglycine generating enzyme''' | ||
| Line 28: | Line 25: | ||
[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
[[Category: Rudolph, M G.]] | [[Category: Rudolph, M G.]] | ||
[[Category: | [[Category: Duf323]] | ||
[[Category: | [[Category: Formylglycine]] | ||
[[Category: | [[Category: Homodimer]] | ||
[[Category: | [[Category: Multiple sulfatase deficiency]] | ||
[[Category: | [[Category: Sulfatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:52:17 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:52, 3 May 2008
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 Page seeded by OCA on Sat May 3 15:52:17 2008
