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Structural analysis and comparison of the C‐terminal transport signal domains of hemolysin A and leukotoxin A
Author(s) -
Yin Ya,
Zhang Fang,
Ling Victor,
Arrowsmith Cheryl H.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00454-h
Subject(s) - hemolysin , chemistry , transporter , homology (biology) , biophysics , signal peptide , nuclear magnetic resonance spectroscopy , toxin , biochemistry , peptide sequence , biology , stereochemistry , amino acid , gene , virulence
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 α‐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.