1z70: Difference between revisions

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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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1z70, resolution 1.15Å" />

'''1.15A resolution structure of the formylglycine generating enzyme FGE'''<br />

==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.

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==

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==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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Z70 OCA].

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==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Rudolph, M.G.]]

[[Category: Rudolph, M G.]]

[[Category: CA]]

[[Category: CL]]

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[[Category: multiple sulfatase deficiency]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 20:~~30:21 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:40 2008''

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@@ Line 1: / Line 1: @@
-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1z70, resolution 1.15&Aring;" />
 '''1.15A resolution structure of the formylglycine generating enzyme FGE'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-Z70 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z70 OCA].
+Z70 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==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Rudolph, M.G.]]
+[[Category: Rudolph, M G.]]
 [[Category: CA]]
 [[Category: CL]]
@@ Line 25: / Line 24: @@
 [[Category: multiple sulfatase deficiency]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:30:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:40 2008''