Solution Structure of the E.coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain

Deprez, Christophe; Lloubès, Roland; Gavioli, Marthe; Marion, Dominique; Guerlesquin, Françoise; Blanchard, Laurence

doi:10.1016/j.jmb.2004.12.028

Cited by 64 publications

(78 citation statements)

References 35 publications

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“…71,2007 COLICIN BIOLOGY 179 interacts with major porins and the TolB-Pal complex (see below). The C-terminal domain, which constitutes the site of colicin binding, presents a more globular fold (148,421,677). TolB is a periplasmic protein that peripherally associates with the outer membrane (291).…”

Section: Tol-dependent Colicinsmentioning

confidence: 99%

“…7). The structure of the TolA C-terminal domain has been solved by both crystallography and NMR, alone and in association with partner domains (148,421,553,677). It forms a novel fold consisting of three antiparallel ␤-strands with four helical motifs (Fig.…”

Section: Tol-dependent Colicinsmentioning

confidence: 99%

“…This probably suggests that molecular recognition involves concerted binding and folding events that occur simultaneously. It has been further suggested that this might be done through "induced-fit" (e.g., recognition of the ligand induces a conformational modification and subsequent high-affinity binding) or "preexistingequilibrium" (e.g., distinct structural conformations of the Tol subunit or colicin N-terminal domains exist, with one of them with high affinity for the ligand) mechanisms (148). However, no structural modifications of the TolA C-terminal domain have been observed upon binding of the colicin N N-terminal domain (5), thus reflecting different behaviors of TolA with different partners.…”

Section: Tol-dependent Colicinsmentioning

confidence: 99%

“…However, the degradation pattern is quite different, suggesting that proteolytic cleavage is not identical (Barnéoud et al, unpublished). Indeed, the addition of the purified g3p-N1 domain on labeled TolAIII molecules induces weak structural changes of the TolA C-terminal domain (148), demonstrating that if both colicins and g3p N-terminal domains interact with TolAIII, and if both interactions involve a similar tetrapeptide motif, the mode of interaction is likely to be different. Conversely, the addition of TolAIII on labeled g3p-N1 showed chemical shifts indicative of conformational modifications within the g3p molecule (148,553).…”

Section: Translocation Of Phage Dnamentioning

confidence: 99%

“…Indeed, the addition of the purified g3p-N1 domain on labeled TolAIII molecules induces weak structural changes of the TolA C-terminal domain (148), demonstrating that if both colicins and g3p N-terminal domains interact with TolAIII, and if both interactions involve a similar tetrapeptide motif, the mode of interaction is likely to be different. Conversely, the addition of TolAIII on labeled g3p-N1 showed chemical shifts indicative of conformational modifications within the g3p molecule (148,553). Competition between the g3p-N2 and the TolA C-terminal domains is suggested by NMR analyses showing that the addition of purified g3p-N2 on labeled g3p-N1 induces identical modifications (553).…”

Section: Translocation Of Phage Dnamentioning

confidence: 99%

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Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

984

1,324

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SUMMARY Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

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Section: Tol-dependent Colicinsmentioning

confidence: 99%

Section: Tol-dependent Colicinsmentioning

confidence: 99%

Section: Tol-dependent Colicinsmentioning

confidence: 99%

Section: Translocation Of Phage Dnamentioning

confidence: 99%

Section: Translocation Of Phage Dnamentioning

confidence: 99%

See 3 more Smart Citations

Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

984

1,324

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Chemically Synthesized 58‐mer LysM Domain Binds Lipochitin Oligosaccharide

et al. 2014

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Recognition of carbohydrates by proteins is a ubiquitous biochemical process. In legume-rhizobium symbiosis, lipochitin oligosaccharides, also referred to as nodulation (nod) factors, function as primary rhizobial signal molecules to trigger root nodule development. Perception of these signal molecules is receptor mediated, and nod factor receptor 5 (NFR5) from the model legume Lotus japonicus is predicted to contain three LysM domain binding sites. Here we studied the interactions between nod factor and each of the three NFR5 LysM domains, which were chemically synthesized. LysM domain variants (up to 58 amino acids) designed to optimize solubility were chemically assembled by solid-phase peptide synthesis (SPPS) with microwave heating. Their interaction with nod factors and chitin oligosaccharides was studied by isothermal titration calorimetry and circular dichroism (CD) spectroscopy. LysM2 showed a change in folding upon nod factor binding, thus providing direct evidence that the LysM domain of NFR5 recognizes lipochitin oligosaccharides. These results clearly show that the L. japonicus LysM2 domain binds to the nod factor from Mesorhizobium loti, thereby causing a conformational change in the LysM2 domain. The preferential affinity for nod factors over chitin oligosaccharides was demonstrated by a newly developed glycan microarray. Besides the biological implications, our approach shows that carbohydrate binding to a small protein domain can be detected by CD spectroscopy.

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Design of a Highly Efficient O₂ Cathode Based on Bilirubin Oxidase from Magnaporthe oryzae

et al. 2013

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Solution Structure of the E.coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain

Cited by 64 publications

References 35 publications

Colicin Biology

Colicin Biology

Chemically Synthesized 58‐mer LysM Domain Binds Lipochitin Oligosaccharide

Design of a Highly Efficient O₂ Cathode Based on Bilirubin Oxidase from Magnaporthe oryzae

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Solution Structure of the E.coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain

Cited by 64 publications

References 35 publications

Colicin Biology

Colicin Biology

Chemically Synthesized 58‐mer LysM Domain Binds Lipochitin Oligosaccharide

Design of a Highly Efficient O2 Cathode Based on Bilirubin Oxidase from Magnaporthe oryzae

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Product

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About

Design of a Highly Efficient O₂ Cathode Based on Bilirubin Oxidase from Magnaporthe oryzae