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 <scene name='80/801257/Cv/5'>making numerous interactions with the protein</scene><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/6'>Cl coordination site</scene>.
*<scene name='80/801257/Cv/14'>Cl coordination site</scene>. Water molecules are shown as red spheres.
*<scene name='80/801257/Cv/7'>1st Ca coordination site</scene>.
*<scene name='80/801257/Cv/15'>1st Ca coordination site</scene>.
*<scene name='80/801257/Cv/8'>2nd 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 />

Latest revision as of 11:54, 7 December 2023


Function

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[1].

Disease

Mutations in SUMF1 cause multiple sulfatase deficiency - a lysosomal storage disorder. SUMF1 is associated with chronic obstructive pulmonary disease[2].

Structural highlights

. The structure of SUMF1 complex with its substrate sulfatase terminal peptide CTPSR. . Cys341 was found to be to the peptide cysteine residue. The peptide binds at the surface of SUMF1 in an extended conformation [3].

  • . Water molecules are shown as red spheres.
  • .
  • .

Glycosylated human sulfatase-modifying factor 1 (cyan) complex with arylsulfatase peptide (magenta), Ca+2 ion (green) and Cl- ion (green) (PDB code 2aij)

Drag the structure with the mouse to rotate

3D structures of sulfatase-modifying factor3D structures of sulfatase-modifying factor

Updated on 07-December-2023

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

ReferencesReferences

  1. ↑ Zito E, Buono M, Pepe S, Settembre C, Annunziata I, Surace EM, Dierks T, Monti M, Cozzolino M, Pucci P, Ballabio A, Cosma MP. Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum. EMBO J. 2007 May 16;26(10):2443-53. doi: 10.1038/sj.emboj.7601695. Epub 2007 Apr , 19. PMID:17446859 doi:http://dx.doi.org/10.1038/sj.emboj.7601695
  2. ↑ Weidner J, Jarenback L, de Jong K, Vonk JM, van den Berge M, Brandsma CA, Boezen HM, Sin D, Bosse Y, Nickle D, Ankerst J, Bjermer L, Postma DS, Faiz A, Tufvesson E. Sulfatase modifying factor 1 (SUMF1) is associated with Chronic Obstructive Pulmonary Disease. Respir Res. 2017 May 2;18(1):77. doi: 10.1186/s12931-017-0562-5. PMID:28464818 doi:http://dx.doi.org/10.1186/s12931-017-0562-5
  3. ↑ Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG. A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. Proc Natl Acad Sci U S A. 2006 Jan 3;103(1):81-6. Epub 2005 Dec 20. PMID:16368756

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

Michal Harel, Alexander Berchansky
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