FEBS Letters
Volume 584, Issue 8 , Pages 1521-1525, 16 April 2010

QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains

Edited by Kaspar Locher

  • Assaf Alon

      Affiliations

    • Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
    • ,
  • Erin J. Heckler

      Affiliations

    • Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA
    • ,
  • Colin Thorpe

      Affiliations

    • Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA
    • ,
  • Deborah Fass

      Affiliations

    • Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
    • Corresponding Author InformationCorresponding author. Fax: +972 8 934 4136.

Received 31 January 2010; received in revised form 2 March 2010; accepted 2 March 2010. published online 10 March 2010.

Abstract 

Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins. Human QSOX1 is a multi-domain, monomeric enzyme containing a module related to the single-domain sulfhydryl oxidases of the Erv family. A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes. However, one pseudo-dimer “subunit” has lost its cofactor and catalytic activity. In QSOX evolution, a further concatenation to a member of the protein disulfide isomerase family resulted in an enzyme capable of both disulfide formation and efficient transfer to substrate proteins.

Keywords: Disulfide bond formation, Domain duplication, Domain fusion, Flavin adenine dinucleotide, Sulfhydryl oxidase

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PII: S0014-5793(10)00194-8

doi:10.1016/j.febslet.2010.03.001

FEBS Letters
Volume 584, Issue 8 , Pages 1521-1525, 16 April 2010

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