TRANSPORT PROTEIN / Type VI secretion system / TssA
Function / homology
Type VI secretion system-associated, VCA0119 / Type VI secretion, EvfE, EvfF, ImpA, BimE, VC_A0119, VasJ / ImpA, N-terminal / ImpA, N-terminal, type VI secretion system / identical protein binding / ImpA N-terminal domain-containing protein / Type VI secretion protein
Function and homology information
Biological species
Escherichia coli 042 (bacteria)
Method
X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.35 Å
Journal: Nature / Year: 2016 Title: Priming and polymerization of a bacterial contractile tail structure. Authors: Abdelrahim Zoued / Eric Durand / Yannick R Brunet / Silvia Spinelli / Badreddine Douzi / Mathilde Guzzo / Nicolas Flaugnatti / Pierre Legrand / Laure Journet / Rémi Fronzes / Tâm Mignot / ...Authors: Abdelrahim Zoued / Eric Durand / Yannick R Brunet / Silvia Spinelli / Badreddine Douzi / Mathilde Guzzo / Nicolas Flaugnatti / Pierre Legrand / Laure Journet / Rémi Fronzes / Tâm Mignot / Christian Cambillau / Eric Cascales / Abstract: Contractile tails are composed of an inner tube wrapped by an outer sheath assembled in an extended, metastable conformation that stores mechanical energy necessary for its contraction. Contraction ...Contractile tails are composed of an inner tube wrapped by an outer sheath assembled in an extended, metastable conformation that stores mechanical energy necessary for its contraction. Contraction is used to propel the rigid inner tube towards target cells for DNA or toxin delivery. Although recent studies have revealed the structure of the contractile sheath of the type VI secretion system, the mechanisms by which its polymerization is controlled and coordinated with the assembly of the inner tube remain unknown. Here we show that the starfish-like TssA dodecameric complex interacts with tube and sheath components. Fluorescence microscopy experiments in enteroaggregative Escherichia coli reveal that TssA binds first to the type VI secretion system membrane core complex and then initiates tail polymerization. TssA remains at the tip of the growing structure and incorporates new tube and sheath blocks. On the basis of these results, we propose that TssA primes and coordinates tail tube and sheath biogenesis.
Mass: 18.015 Da / Num. of mol.: 146 / Source method: isolated from a natural source / Formula: H2O
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION
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Sample preparation
Crystal
Density Matthews: 3.4 Å3/Da / Density % sol: 64 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.8 Details: 300 nL of protein at 4.7 mg/mL with 100 nL of 20% PEG 8000, 0.2M Calcium Acetate, 0.1 M MES pH 6.8
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