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000023152 1001_ $$0P:(DE-Juel1)VDB94799$$aLecher, J.$$b0$$uFZJ
000023152 245__ $$aAn RTX toxin transporters tether ist substrate prior to secretion via the unique function of ist N- terminal domain
000023152 260__ $$aLondon [u.a.]$$bElsevier Science$$c2012
000023152 300__ $$a1778 - 1787
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000023152 520__ $$aType 1 secretion systems (T1SS) catalyze the one step protein transport across the membranes of Gram-negative bacteria and are composed of an outer membrane protein, a membrane fusion protein and an ABC transporter. The ABC transporter consists of the canonical nucleotide binding and transmembrane domains. For the toxin hemolysin A (HlyA), the ABC transporter HlyB carries an additional, N-terminal domain sharing about 40% homology to C39 peptidases, but this "C39-like domain" (CLD) is suggested to feature another, yet unknown function. Our functional and structural analysis demonstrates that the CLD is essential for secretion and that it specifically interacts with the unfolded state of HlyA. We determined the nuclear magnetic resonance structure of the CLD as well as the substrate-binding region within the CLD. This mode of action, represents a mechanism within T1SS and answers the question, how a large and unfolded substrate is protected inside the cells during secretion.
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000023152 7001_ $$0P:(DE-HGF)0$$aSchwarz, C.K.W.$$b1
000023152 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b2$$uFZJ
000023152 7001_ $$0P:(DE-HGF)0$$aSmits, S.H.J.$$b3
000023152 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000023152 7001_ $$0P:(DE-HGF)0$$aSchmitt, L.$$b5
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000023152 8567_ $$uhttp://dx.doi.org/10.1016/j.str.2012.08.005
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