Sulfatase-modifying factor: Difference between revisions

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<StructureSection load='2aij' size='340' side='right' caption='Glycosylated human sulfatase-modifying factor 1 (grey) complex with arylsulfatase peptide (green), Ca+2 ion (green) and Cl- ion (green) (PDB code [[2aij]]) ' scene=''>
<StructureSection load='2aij' size='400' side='right' caption='Glycosylated human sulfatase-modifying factor 1 (cyan) complex with arylsulfatase peptide (magenta), Ca+2 ion (green) and Cl- ion (green) (PDB code [[2aij]]) ' scene='80/801257/Cv/1'>


== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==


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<ref>PMID:16368756</ref>.
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<ref>PMID:16368756</ref>.


</StructureSection>
</StructureSection>