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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} |
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| [[2aii]] - hSUMF-1 - human<br /> | | [[2aii]], [[1y1e]], [[1y1g]], [[1y1f]], [[1y1j]], [[1y1i]], [[1z70]], [[1y1h]] - hSUMF-1 - human<br /> |
| [[2aft]], [[2afy]], [[2hib]], [[2hi8]] - hSUMF-1 (mutant) <br /> | | [[2aft]], [[2afy]], [[2hib]], [[2hi8]] - hSUMF-1 (mutant) <br /> |
| [[2aij]], [[2aik]] - hSUMF-1 (mutant) + peptide<br /> | | [[2aij]], [[2aik]] - hSUMF-1 (mutant) + peptide<br /> |
Revision as of 11:03, 12 November 2020
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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
Glycosylated human sulfatase-modifying factor 1 complex with arylsulfatase peptide, Ca+2 ion and Cl- ion. The structure of SUMF1 complex with its substrate sulfatase terminal peptide CTPSR. SUMF1 active site contains 2 cysteine residues and mutating either of them to serine results in an inactive enzyme. Cys341 was found to be responsible for substrate binding and makes a Cys-Cys bond to the peptide cysteine residue. The peptide binds at the surface of SUMF1 in an extended conformation making numerous interactions with the protein[3].
- ↑ 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:https://dx.doi.org/10.1038/sj.emboj.7601695
- ↑ 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:https://dx.doi.org/10.1186/s12931-017-0562-5
- ↑ 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
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3D structures of sulfatase-modifying factor
Updated on 12-November-2020
Sulfatase, 1y1e, 1y1g, 1y1f, 1y1j, 1y1i, 1z70, 1y1h - hSUMF-1 - human
2aft, 2afy, 2hib, 2hi8 - hSUMF-1 (mutant)
2aij, 2aik - hSUMF-1 (mutant) + peptide
1y4j - hSUMF-2
References
