3LLK

Sulfhydryl Oxidase Fragment of Human QSOX1

3LLK の概要

• エントリーDOI: 10.2210/pdb3llk/pdb
• 関連するPDBエントリー: 1JR8 1JRA 1OQC 2HJ3 3GWL 3GWN 3LLI
• 分子名称: Sulfhydryl oxidase 1, FLAVIN-ADENINE DINUCLEOTIDE, CITRATE ANION, ... (4 entities in total)
• 機能のキーワード: sulfhydryl oxidase, disulfide, flavin adenine dinucleotide, alternative splicing, fad, flavoprotein, glycoprotein, golgi apparatus, membrane, oxidoreductase, polymorphism, secreted, transmembrane
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Golgi apparatus membrane; Single- pass membrane protein. Isoform 2: Secreted, extracellular space: O00391
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91919.99

構造登録者

Alon, A.,Fass, D. (登録日: 2010-01-29, 公開日: 2010-03-31, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)