1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB) |
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Authors: | Justin Lecher Matthias Stoldt Christian K W Schwarz Sander H J Smits Lutz Schmitt Dieter Willbold |
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Institution: | (1) Institute of Structural Biochemistry (ICS-6), Research Centre Juelich, Juelich, Germany;(2) Institut f?r Physikalische Biologie, Heinrich-Heine-Universitaet Duesseldorf, Duesseldorf, Germany;(3) Institut f?r Biochemie, Heinrich-Heine-Universitaet Duesseldorf, Duesseldorf, Germany; |
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Abstract: | ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins, which catalyze the translocation of molecules
across biological membranes in an ATP-dependent manner. Despite the diversity in the transported substrates, they all share
the same architecture, comprised of two transmembrane (TMD) and two nucleotide-binding domains (NBD). Members of the bacteriocin
ABC transporter subfamily feature a special domain, belonging to the C39 (cystein protease family 39) peptidase protein family.
These domains are assumed to cleave a C-terminal signal sequence from the protein or peptide substrate before or during the
transport process. Although the C39 peptidase-like domain of the ABC transporter haemolysin B from E. coli shows no proteolytic activity, it is essential for the function of this transporter. In order to elucidate the contribution
of the isolated C39 peptidase-like domain in the whole transport process, the backbone and side chain 1H, 15N and 13C-NMR chemical shifts have been assigned. |
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