1z70
From Proteopedia
(New page: 200px<br /> <applet load="1z70" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z70, resolution 1.15Å" /> '''1.15A resolution st...) |
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| - | [[Image:1z70.gif|left|200px]]<br /> | + | [[Image:1z70.gif|left|200px]]<br /><applet load="1z70" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1z70" size=" | + | |
caption="1z70, resolution 1.15Å" /> | caption="1z70, resolution 1.15Å" /> | ||
'''1.15A resolution structure of the formylglycine generating enzyme FGE'''<br /> | '''1.15A resolution structure of the formylglycine generating enzyme FGE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sulfatases are a family of enzymes essential for the degradation of | + | Sulfatases are a family of enzymes essential for the degradation of sulfate esters. Formylglycine is the key catalytic residue in the active site of sulfatases and is generated from a cysteine residue by FGE, the formylglycine-generating enzyme. Inactivity of FGE owing to inherited mutations in the FGE gene results in multiple sulfatase deficiency (MSD), which leads to early death in infants. Human FGE was crystallized in the presence of traces of the protease elastase, which was absolutely essential for crystal growth, and the structure of FGE was determined by molecular replacement. Before this model was completed, the FGE structure was re-determined by SAD phasing using in-house data based on the anomalous signal of two calcium ions bound to the native enzyme and intrinsic S atoms. A 14-atom substructure was determined at 1.8 A resolution by SHELXD; SHELXE was used for density modification and phase extension to 1.54 A resolution. Automated model building with ARP/wARP and refinement with REFMAC5 yielded a virtually complete model without manual intervention. The minimal data requirements for successful phasing and the relative contributions of the Ca and S atoms are discussed and compared with the related FGE paralogue, pFGE. This work emphasizes the usefulness of de novo phasing using weak anomalous scatterers and in-house data. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z70 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, CL and CXS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Z70 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>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CXS:'>CXS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z70 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M G.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: multiple sulfatase deficiency]] | [[Category: multiple sulfatase deficiency]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:40 2008'' |
Revision as of 14:12, 21 February 2008
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1.15A resolution structure of the formylglycine generating enzyme FGE
Contents |
Overview
Sulfatases are a family of enzymes essential for the degradation of sulfate esters. Formylglycine is the key catalytic residue in the active site of sulfatases and is generated from a cysteine residue by FGE, the formylglycine-generating enzyme. Inactivity of FGE owing to inherited mutations in the FGE gene results in multiple sulfatase deficiency (MSD), which leads to early death in infants. Human FGE was crystallized in the presence of traces of the protease elastase, which was absolutely essential for crystal growth, and the structure of FGE was determined by molecular replacement. Before this model was completed, the FGE structure was re-determined by SAD phasing using in-house data based on the anomalous signal of two calcium ions bound to the native enzyme and intrinsic S atoms. A 14-atom substructure was determined at 1.8 A resolution by SHELXD; SHELXE was used for density modification and phase extension to 1.54 A resolution. Automated model building with ARP/wARP and refinement with REFMAC5 yielded a virtually complete model without manual intervention. The minimal data requirements for successful phasing and the relative contributions of the Ca and S atoms are discussed and compared with the related FGE paralogue, pFGE. This work emphasizes the usefulness of de novo phasing using weak anomalous scatterers and in-house data.
Disease
Known disease associated with this structure: Multiple sulfatase deficiency OMIM:[607939]
About this Structure
1Z70 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
De novo calcium/sulfur SAD phasing of the human formylglycine-generating enzyme using in-house data., Roeser D, Dickmanns A, Gasow K, Rudolph MG, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1057-66. Epub 2005, Jul 20. PMID:16041070
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