Structural highlights
3lli is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 1jr8, 1jra, 2hj3, 3gwn, 3gwl, 1oqc, 3llk |
| Gene: | QSCN6, QSOX1, UNQ2520/PRO6013 (Homo sapiens) |
| Activity: | Thiol oxidase, with EC number 1.8.3.2 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.,Alon A, Heckler EJ, Thorpe C, Fass D FEBS Lett. 2010 Apr 16;584(8):1521-5. Epub 2010 Mar 6. PMID:20211621[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alon A, Heckler EJ, Thorpe C, Fass D. QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains. FEBS Lett. 2010 Apr 16;584(8):1521-5. Epub 2010 Mar 6. PMID:20211621 doi:10.1016/j.febslet.2010.03.001
