Legionella pneumophilautilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization
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چکیده
منابع مشابه
Disulfide bond isomerization in prokaryotes.
Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes.
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extracytoplasmic environments (e.g., the lumen of the eukaryotic endoplasmic reticulum and the gram-negative bacterial periplasmic space). In contrast, the cytoplasm displays a network of enzymes and molecules dedicated to the reduction of disulfide bonds (Åslund Laurent Debarbieux and Jon Beckwith* Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 0...
متن کاملDisulfide Bond Oxidoreductase DsbA 2 of Legionella pneumophila 2 Exhibits Protein Disulfide Isomerase Activity 3
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Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity.
The extracytoplasmic assembly of the Dot/Icm type IVb secretion system (T4SS) of Legionella pneumophila is dependent on correct disulfide bond (DSB) formation catalyzed by a novel and essential disulfide bond oxidoreductase DsbA2 and not by DsbA1, a second nonessential DSB oxidoreductase. DsbA2, which is widely distributed in the microbial world, is phylogenetically distinct from the canonical ...
متن کاملCatalysis of protein disulfide bond isomerization in a homogeneous substrate.
Protein disulfide isomerase (PDI) catalyzes the rearrangement of nonnative disulfide bonds in the endoplasmic reticulum of eukaryotic cells, a process that often limits the rate at which polypeptide chains fold into a native protein conformation. The mechanism of the reaction catalyzed by PDI is unclear. In assays involving protein substrates, the reaction appears to involve the complete reduct...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2015
ISSN: 0950-382X
DOI: 10.1111/mmi.12914