PMID:18189304
| Citation |
Renn, JP and Clark, PL (2008) A conserved stable core structure in the passenger domain beta-helix of autotransporter virulence proteins. Biopolymers 89:420-7 |
|---|---|
| Abstract |
In Gram-negative bacteria, a wide variety of virulence factors are secreted via the autotransporter (AT) pathway. Intriguingly, there is no significant concentration of ATP in the periplasm, nor a proton gradient across the OM, so the energetic origin of efficient secretion of AT proteins is unknown. More than 97% of AT proteins are predicted to contain right-handed parallel beta-helical structure, and the three crystal structures available for AT passenger domains each contain a long right-handed parallel beta-helix. Previous studies have shown that pertactin, an AT from Bordetella pertussis, exhibits three-state folding and has a C-terminal stable core structure. Here, we show that Pet, an unrelated AT from Escherichia coli, also exhibits three-state unfolding and also has a stable core structure. Deletion mutants, mass spectrometry, and N-terminal sequencing demonstrate that the Pet stable core is also located near the C-terminus of the passenger domain. Moreover, sequence analysis suggests that three-state folding and a C-terminal stable core structure could be important general features of the biogenesis of AT proteins in vivo. |
| Links |
PubMed Online version:10.1002/bip.20924 |
| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Toxins/chemistry; Bacterial Toxins/genetics; Conserved Sequence; Electrophoresis, Polyacrylamide Gel; Endopeptidase K/chemistry; Enterotoxins/chemistry; Enterotoxins/genetics; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Guanidine/chemistry; Models, Molecular; Molecular Sequence Data; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Serine Endopeptidases; Virulence Factors/chemistry; Virulence Factors/genetics; Virulence Factors, Bordetella/chemistry; Virulence Factors, Bordetella/genetics |
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