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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS I02-Macromolecular Crystallography Data acquisition Diagnostics Health Physics	Structural and biophysical analysis of nuclease protein antibiotics Alexander Klein , Justyna Wojdyla , Amar Joshi , Inokentijs Josts , L. C. Mccaughey , N. Housden , R. Kaminska , Olwyn Byron , D. Walker , C. Kleanthous Biochemical Journal DOI: 10.1042/BCJ20160544 Diamond Proposal Number(s): [12346] Open Access Show Abstract ▼ Abstract: Protein antibiotics (bacteriocins) are a large and diverse family of multidomain toxins that kill specific Gram-negative bacteria during intraspecies competition for resources. Our understanding of the mechanism of import of such potent toxins has increased significantly in recent years especially with the reporting of several structures of bacteriocin domains. Less well understood is the structural biochemistry of intact bacteriocins and how these compare across bacterial species. Here we focus on endonuclease (DNase) bacteriocins that target the genomes of Escherichia coli and Pseudomonas aeruginosa , known as E-type colicins and S-type pyocins, respectively, bound to their specific immunity (Im) proteins. First, we report the 3.2 Å structure of the DNase colicin ColE9 in complex with its ultra-high affinity immunity protein, Im9. In contrast to Im3, which when bound to the ribonuclease (rRNase) domain of the homologous colicin ColE3 makes contact with the translocation (T-) domain of the toxin, we find that Im9 makes no such contact and only interactions with the ColE9 cytotoxic domain are observed. Second, we report small angle X-ray scattering (SAXS) data for two S-type DNase pyocins, S2 and AP41, into which are fitted recently determined X-ray structures for isolated domains. We find that DNase pyocins and colicins are both highly elongated molecules even though the order of their constituent domains differs. We discuss the implications of these architectural similarities and differences in the context of the translocation mechanism of protein antibiotics through the cell envelope of Gram-negative bacteria.	Jul 2016

Instruments / Technical Area

Publication Details

Published

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B21-High Throughput SAXS
I02-Macromolecular Crystallography
Data acquisition
Diagnostics
Health Physics

Structural and biophysical analysis of nuclease protein antibiotics

Alexander Klein , Justyna Wojdyla , Amar Joshi , Inokentijs Josts , L. C. Mccaughey , N. Housden , R. Kaminska , Olwyn Byron , D. Walker , C. Kleanthous

Biochemical Journal

DOI: 10.1042/BCJ20160544

Diamond Proposal Number(s): [12346]