Journal Article

PreJuSER-16637

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Crystallisation and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter Haemolysin B

Schwarz, C. K. W. ; Tschapek, B. ; Jumpertz, T. ; Jenewein, S. ; Lecher, J.FZJ* ; Willbold, D.FZJ* ; Panjikar, S. ; Halland, B. ; Smits, S. H. J. ; Schmitt, L.

2011
Blackwell Oxford [u.a.]

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Please use a persistent id in citations: doi:10.1107/S1744309111010876

Abstract: The ABC transporter haemolysin B (HlyB) from Escherichia coli is part of a type I secretion system that translocates a 110 kDa toxin in one step across both membranes of this Gram-negative bacterium in an ATP-dependent manner. Sequence analysis indicates that HlyB contains a C39 peptidase-like domain at its N-terminus. C39 domains are thiol-dependent peptidases that cleave their substrates after a GG motif. Interestingly, the catalytically invariant cysteine is replaced by a tyrosine in the C39-like domain of HlyB. Here, the overexpression, purification and crystallization of the isolated C39-like domain are described as a first step towards obtaining structural insights into this domain and eventually answering the question concerning the function of a degenerated C39 domain in the ABC transporter HlyB.

Keyword(s): ATP-Binding Cassette Transporters: chemistry (MeSH) ; Bacterial Proteins: chemistry (MeSH) ; Carrier Proteins: chemistry (MeSH) ; Crystallization (MeSH) ; Crystallography, X-Ray (MeSH) ; Escherichia coli: chemistry (MeSH) ; Hemolysin Proteins: chemistry (MeSH) ; Protein Multimerization (MeSH) ; Protein Refolding (MeSH) ; ATP-Binding Cassette Transporters ; Bacterial Proteins ; Carrier Proteins ; Hemolysin Proteins ; Hlyb protein, Bacteria ; J

Note: We would like to acknowledge Solvej Siedler for important assistance during the initial stages of this project. This work was funded by the EDICT (European Initiative on Channels and Transporters) consortium FP7 Theme (Health-2007-2.1.1-5) to BT and LS. We thank the Ministry of Innovation, Science and Research of the German Federal State North Rhine-Westphalia (NRW) and the Heinrich Heine University Dusseldorf (scholarship from the CLIB-Graduate Cluster Industrial Biotechnology to CKWS).

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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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