The Channel Domain of Colicin a Modifies the Dimeric Organization of Its Immunity Protein
نویسندگان
چکیده
Laboratoire d’Ingéniérie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UPR-9027, 13402 Marseille cedex 20, France, and Université de la Méditerranée Aix-Marseille. Running head : Ion channel inhibition Address correspondence to: Denis Duché, Laboratoire d’Ingéniérie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France. Tel. 33 04 91 16 45 61; Fax. 33 04 91 71 21 24: E-Mail: [email protected]
منابع مشابه
Channel domain of colicin A modifies the dimeric organization of its immunity protein.
Proteins conferring immunity against pore-forming colicins are localized in the Escherichia coli inner membrane. Their protective effects are mediated by direct interaction with the C-terminal domain of their cognate colicins. Cai, the immunity protein protecting E. coli against colicin A, contains four cysteine residues. We report cysteine cross-linking experiments showing that Cai forms homod...
متن کاملImmunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement
Nuclease colicins bind their target receptor BtuB in the outer membrane of sensitive Escherichia coli cells in the form of a high-affinity complex with their cognate immunity proteins. The release of the immunity protein from the colicin complex is a prerequisite for cell entry of the colicin and occurs via a process that is still relatively poorly understood. We have previously shown that an e...
متن کاملEvidence that the immunity protein inactivates colicin 5 immediately prior to the formation of the transmembrane channel.
Determination and analysis of the nucleotide sequences of the activity, immunity, and lysis genes of colicin 5 assigned colicin 5 to the subclass of pore-forming colicins to which colicins 10, E1, Ia, Ib, and K belong. Mutational analysis of colicin 5 and exchange of DNA fragments between the most closely related colicins, colicins 5 and 10, and between their immunity proteins localized the reg...
متن کاملThe crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein.
BACKGROUND Colicin E7 (ColE7) is one of the bacterial toxins classified as a DNase-type E-group colicin. The cytotoxic activity of a colicin in a colicin-producing cell can be counteracted by binding of the colicin to a highly specific immunity protein. This biological event is a good model system for the investigation of protein recognition. RESULTS The crystal structure of a one-to-one comp...
متن کاملStructure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone a...
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تاریخ انتشار 2010