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David Veesler – One of the best experts on this subject based on the ideXlab platform.

  • Structure of the type VI secretion system TssK–TssF–TssG Baseplate subcomplex revealed by cryo-electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture. Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 Å cryoEM structure of the E.coli T6SS Baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS Baseplate and needle complex.

  • structure of the type vi secretion system tssk tssf tssg Baseplate subcomplex revealed by cryo electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 A resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture. Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 A cryoEM structure of the E.coli T6SS Baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS Baseplate and needle complex.

  • Structure of the type VI secretion system TssK–TssF–TssG Baseplate subcomplex revealed by cryo-electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture.

Christian Cambillau – One of the best experts on this subject based on the ideXlab platform.

  • Structural Insights into Lactococcal Siphophage p2 Baseplate Activation Mechanism.
    Viruses, 2020
    Co-Authors: Silvia Spinelli, Christian Cambillau, Sylvain Moineau, Denise M. Tremblay, Adeline Goulet

    Abstract:

    Virulent phages infecting L. lactis, an industry-relevant bacterium, pose a significant risk to the quality of the fermented milk products. Phages of the Skunavirus genus are by far the most isolated lactococcal phages in the cheese environments and phage p2 is the model siphophage for this viral genus. The Baseplate of phage p2, which is used to recognize its host, was previously shown to display two conformations by X-ray crystallography, a rested state and an activated state ready to bind to the host. The Baseplate became only activated and opened in the presence of Ca2+. However, such an activated state was not previously observed in the virion. Here, using nanobodies binding to the Baseplate, we report on the negative staining electron microscopy structure of the activated form of the Baseplate directly observed in the p2 virion, that is compatible with the activated Baseplate crystal structure. Analyses of this new structure also established the presence of a second distal tail (Dit) hexamer as a component of the Baseplate, the topology of which differs largely from the first one. We also observed an uncoupling between the Baseplate activation and the tail tip protein (Tal) opening, suggesting an infection mechanism more complex than previously expected.

  • Structure of the type VI secretion system TssK–TssF–TssG Baseplate subcomplex revealed by cryo-electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture. Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 Å cryoEM structure of the E.coli T6SS Baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS Baseplate and needle complex.

  • structure of the type vi secretion system tssk tssf tssg Baseplate subcomplex revealed by cryo electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 A resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture. Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 A cryoEM structure of the E.coli T6SS Baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS Baseplate and needle complex.

Young Jun Park – One of the best experts on this subject based on the ideXlab platform.

  • Structure of the type VI secretion system TssK–TssF–TssG Baseplate subcomplex revealed by cryo-electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture. Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 Å cryoEM structure of the E.coli T6SS Baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS Baseplate and needle complex.

  • structure of the type vi secretion system tssk tssf tssg Baseplate subcomplex revealed by cryo electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 A resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture. Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 A cryoEM structure of the E.coli T6SS Baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS Baseplate and needle complex.

  • Structure of the type VI secretion system TssK–TssF–TssG Baseplate subcomplex revealed by cryo-electron microscopy
    Nature Communications, 2018
    Co-Authors: Young Jun Park, Christian Cambillau, Kaitlyn D. Lacourse, Frank Dimaio, Joseph D. Mougous, David Veesler

    Abstract:

    Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a Baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the Baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli Baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 Baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS Baseplate architecture.