Structural highlights
Function
[HLYB3_ECOLX] Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).
Publication Abstract from PubMed
Type 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.
An RTX Transporter Tethers Its Unfolded Substrate during Secretion via a Unique N-Terminal Domain.,Lecher J, Schwarz CK, Stoldt M, Smits SH, Willbold D, Schmitt L Structure. 2012 Sep 5. PMID:22959622[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lecher J, Schwarz CK, Stoldt M, Smits SH, Willbold D, Schmitt L. An RTX Transporter Tethers Its Unfolded Substrate during Secretion via a Unique N-Terminal Domain. Structure. 2012 Sep 5. PMID:22959622 doi:http://dx.doi.org/10.1016/j.str.2012.08.005
