Journal Article

PreJuSER-16636

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png 1H, 15N and 13³C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB)

Lecher, J.FZJ* ; Stoldt, M.FZJ* ; Schwarz, C. K. W. ; Smits, S. H. J. ; Schmitt, L. ; Willbold, D.FZJ*

2011
Springer Netherlands Dordrecht [u.a.]

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Please use a persistent id in citations: doi:10.1007/s12104-011-9299-0

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 (1)H, (15)N and (13)C-NMR chemical shifts have been assigned.

Keyword(s): ATP-Binding Cassette Transporters: chemistry (MeSH) ; Catalytic Domain (MeSH) ; Escherichia coli: enzymology (MeSH) ; Escherichia coli Proteins: chemistry (MeSH) ; Hemolysin Proteins: chemistry (MeSH) ; Isotopes: chemistry (MeSH) ; Nuclear Magnetic Resonance, Biomolecular (MeSH) ; ATP-Binding Cassette Transporters ; Escherichia coli Proteins ; Hemolysin Proteins ; Isotopes ; hemolysin B ; J ; ABC transporter (auto) ; C39 peptidase-like (auto) ; Heteronuclear NMR (auto) ; Resonance assignment (auto)

Note: We would like to thank Melanie Schwarten for helpful discussions. The research has been funded by a fellowship from the International Helmholtz Research School on Biophysics and Soft Matter ("Biosoft") to Justin Lecher. We thank the Ministry of Innovation, Science, and Research of the German Federal State North Rhine-Westphalia (NRW) and the Heinrich-Heine-Universitaet Duesseldorf (scholarship from the CLIB-Graduate Cluster Industrial Biotechnology for Christian Schwarz).

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2011

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