Sulfatase-modifying factor: Difference between revisions

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== Function ==
== Function ==


'''Sulfatase-modifying factor''' (SUMF) is an enzyme that catalyzes the hydrolysis of sulfate esters by oxidizing posttranslationally a cysteine residue in its substrate [[Sulfatase]] active site to 3-oxoalanine (C-α-formylglycine) residue<ref>PMID:17446859</ref>.
'''Sulfatase-modifying factor''' (SUMF) or '''formylglycine-generating enzyme''' is an enzyme that catalyzes the hydrolysis of sulfate esters by oxidizing posttranslationally a cysteine residue in its substrate [[Sulfatase]] active site to 3-oxoalanine (C-α-formylglycine) residue<ref>PMID:17446859</ref>.


== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==


<scene name='80/801257/Cv/2'>Glycosylated human sulfatase-modifying factor 1 complex with arylsulfatase peptide, Ca+2 ion and Cl- ion</scene>. The structure of SUMF1 complex with its substrate sulfatase terminal peptide CTPSR. <scene name='80/801257/Cv/3'>SUMF1 active site contains 2 cysteine residues and mutating either of them to serine results in an inactive enzyme</scene>. Cys341 was found to be <scene name='80/801257/Cv/4'>responsible for substrate binding and makes a Cys-Cys bond</scene> to the peptide cysteine residue. The peptide binds at the surface of SUMF1 in an extended conformation making numerous interactions with the protein<ref>PMID:16368756</ref>.
<scene name='80/801257/Cv/9'>Glycosylated human sulfatase-modifying factor 1 complex with arylsulfatase peptide, Ca+2 ion and Cl- ion</scene>. The structure of SUMF1 complex with its substrate sulfatase terminal peptide CTPSR. <scene name='80/801257/Cv/10'>SUMF1 active site contains 2 cysteine residues and mutating either of them to serine results in an inactive enzyme</scene>. Cys341 was found to be <scene name='80/801257/Cv/11'>responsible for substrate binding and makes a Cys-Cys bond</scene> to the peptide cysteine residue. The peptide binds at the surface of SUMF1 in an extended conformation <scene name='80/801257/Cv/13'>making numerous interactions with the protein</scene><ref>PMID:16368756</ref>.
 
*<scene name='80/801257/Cv/14'>Cl coordination site</scene>. Water molecules are shown as red spheres.
*<scene name='80/801257/Cv/15'>1st Ca coordination site</scene>.
*<scene name='80/801257/Cv/16'>2nd Ca coordination site</scene>.
</StructureSection>
</StructureSection>


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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}


[[2aii]] - hSUMF-1 - human<br />
[[2aii]], [[1y1e]], [[1y1g]], [[1y1f]], [[1y1j]], [[1y1i]], [[1z70]], [[1y1h]], [[5ssy]], [[5ssz]] - hSUMF-1 - human<br />
[[2aft]], [[2afy]], [[2hib]], [[2hi8]] - hSUMF-1 (mutant) <br />
[[2aft]], [[2afy]], [[2hib]], [[2hi8]], [[5ssx]], [[8aru]] - hSUMF-1 (mutant) <br />
[[2aij]], [[2aik]] - hSUMF-1 (mutant) + peptide<br />
[[2aij]], [[2aik]] - hSUMF-1 (mutant) + peptide<br />
[[1y4j]] - hSUMF-2  <br />
[[1y4j]] - hSUMF-2  <br />

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky