Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A.
NMR spectroscopy was used to study the structure of the C-terminal signal sequences of the bacterial toxins, hemolysin A(HlyA) and leukotoxin A (LktA). The two signals share little sequence homology; however, both can direct toxin transport with equal efficiency. We report here that in a membrane mimetic environment both peptides form two short non-interacting alpha-helices separated by a short loop. This higher order structure may be a common feature of C-terminal signals and may be required for interaction with the membrane associated transporter complex.
Yin
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Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.
Zhang
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Ling
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Arrowsmith
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins; D005098:Exotoxins / Q000737:chemistry* / Q000235:genetics; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D016978:Mannheimia haemolytica / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009154:Mutation; D021382:Protein Sorting Signals / Q000737:chemistry / Q000235:genetics; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D005098:Exotoxins; D006460:Hemolysin Proteins; C036507:Hlya protein, E coli; D021382:Protein Sorting Signals; C018579:leukotoxin