Introduction of a Lethal Redox Switch That Controls the Opening and Closing of the Hydrophobic Cavity in LolA

LolA plays a critical role in the outer membrane sorting of Escherichia coli lipoproteins because it carries a hydrophobic lipoprotein from the inner membrane through the hydrophilic periplasm to the outer membrane receptor LolB. LolA has an incomplete β-barrel structure composed of 11 β-strands wit...

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Veröffentlicht in:	The Journal of biological chemistry 2008-09, Vol.283 (37), p.25421-25427
Hauptverfasser:	Watanabe, Shoji, Oguchi, Yuki, Takeda, Kazuki, Miki, Kunio, Tokuda, Hajime
Format:	Artikel
Sprache:	eng
Schlagworte:	Cross-Linking Reagents - chemistry Cysteine - chemistry Disulfides Escherichia coli - metabolism Escherichia coli Proteins - chemistry Lipoproteins - chemistry Models, Chemical Mutation Oxidation-Reduction Periplasmic Binding Proteins - chemistry Phenotype Plasmids - metabolism Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Time Factors
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