3LLI

Sulfhydryl Oxidase Fragment of Human QSOX1

Summary for 3LLI

• Entry DOI: 10.2210/pdb3lli/pdb
• Related: 1JR8 1JRA 1OQC 2HJ3 3GWL 3GWN 3LLK
• Descriptor: Sulfhydryl oxidase 1, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: sulfhydryl oxidase, flavin adenine dinucleotide, disulfide, fad, flavoprotein, glycoprotein, golgi apparatus, oxidoreductase, secreted
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Golgi apparatus membrane; Single- pass membrane protein. Isoform 2: Secreted, extracellular space: O00391
• Total number of polymer chains: 1
• Total formula weight: 30576.96

Authors

Alon, A.,Fass, D. (deposition date: 2010-01-29, release date: 2010-03-23, Last modification date: 2011-07-13)

Primary citation

Alon, A.,Heckler, E.J.,Thorpe, C.,Fass, D.
QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.
Febs Lett., 584:1521-1525, 2010

PubMed 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.

PubMed: 20211621
DOI: 10.1016/j.febslet.2010.03.001

Experimental method

X-RAY DIFFRACTION (2.05 Å)