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Sjors H W Scheres - One of the best experts on this subject based on the ideXlab platform.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Hendrik W Van Veen, Ulrich Zachariae, Sjors H W Scheres, Ben F Luisi
    Abstract:

    The MacA–MacB–TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. Cryo-electron microscopy of the tripartite MacA–MacB–TolC multidrug transporter.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Hendrik W. Van Veen, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Ulrich Zachariae, Xiao Chen Bai, Sjors H W Scheres
    Abstract:

    The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism.

A W P Fitzpatrick - One of the best experts on this subject based on the ideXlab platform.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Hendrik W Van Veen, Ulrich Zachariae, Sjors H W Scheres, Ben F Luisi
    Abstract:

    The MacA–MacB–TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. Cryo-electron microscopy of the tripartite MacA–MacB–TolC multidrug transporter.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Hendrik W. Van Veen, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Ulrich Zachariae, Xiao Chen Bai, Sjors H W Scheres
    Abstract:

    The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism.

Mikael Rhen - One of the best experts on this subject based on the ideXlab platform.

  • Modulation of Biofilm-Formation in Salmonella enterica Serovar Typhimurium by the Periplasmic DsbA/DsbB Oxidoreductase System Requires the GGDEF-EAL Domain Protein STM3615
    2016
    Co-Authors: Naeem Anwar, Syed Fazle Rouf, Mikael Rhen
    Abstract:

    In Salmonella enterica serovar Typhimurium (S. Typhimurium), biofilm-formation is controlled by the cytoplasmic intracellular small-molecular second messenger cyclic 39, 59-di- guanosine monophosphate (c-di-GMP) through the activities of GGDEF and EAL domain Proteins. Here we describe that deleting either dsbA or dsbB, respectively encoding a Periplasmic Protein disulfide oxidase and a cytoplasmic membrane disulfide oxidoreductase, resulted in increased biofilm-formation on solid medium. This increased biofilm-formation, defined as a red, dry and rough (rdar) colony morphotype, paralleled with enhanced expression of the biofilm master regulator CsgD and the biofilm-associated fimbrial subunit CsgA. Deleting csgD in either dsb mutant abrogated the enhanced biofilm-formation. Likewise, overexpression of the c-di-GMP phosphodies-terase YhjH, or mutationally inactivating the CsgD activator EAL-domain Protein YdiV, reduced biofilm-formation in either of the dsb mutants. Intriguingly, deleting the GGDEF-EAL domain Protein gene STM3615 (yhjK), previously not connected to rdar morphotype development, also abrogated the escalated rdar morphotype formation in dsb mutant backgrounds. Enhanced biofilm-formation in dsb mutants was furthermore annulled by exposure to the Protein disulfide catalyst copper chloride. When analyzed for the effect of exogenous reducing stress on biofilm-formation, both dsb mutants initially showed an escalated rdar morphotype development that later dissolved to reveal a smooth mucoid colony morphotype. From these results we conclude that biofilm-development in S. Typhimurium is affected by Periplasmic Protein disulphide bond statu

  • Modulation of biofilm-formation in Salmonella enterica serovar Typhimurium by the Periplasmic DsbA/DsbB oxidoreductase system requires the GGDEF-EAL domain Protein STM3615.
    PLoS ONE, 2014
    Co-Authors: Naeem Anwar, Ute Römling, Syed Fazle Rouf, Mikael Rhen
    Abstract:

    In Salmonella enterica serovar Typhimurium (S. Typhimurium), biofilm-formation is controlled by the cytoplasmic intracellular small-molecular second messenger cyclic 3′, 5′-di- guanosine monophosphate (c-di-GMP) through the activities of GGDEF and EAL domain Proteins. Here we describe that deleting either dsbA or dsbB, respectively encoding a Periplasmic Protein disulfide oxidase and a cytoplasmic membrane disulfide oxidoreductase, resulted in increased biofilm-formation on solid medium. This increased biofilm-formation, defined as a red, dry and rough (rdar) colony morphotype, paralleled with enhanced expression of the biofilm master regulator CsgD and the biofilm-associated fimbrial subunit CsgA. Deleting csgD in either dsb mutant abrogated the enhanced biofilm-formation. Likewise, overexpression of the c-di-GMP phosphodiesterase YhjH, or mutationally inactivating the CsgD activator EAL-domain Protein YdiV, reduced biofilm-formation in either of the dsb mutants. Intriguingly, deleting the GGDEF-EAL domain Protein gene STM3615 (yhjK), previously not connected to rdar morphotype development, also abrogated the escalated rdar morphotype formation in dsb mutant backgrounds. Enhanced biofilm-formation in dsb mutants was furthermore annulled by exposure to the Protein disulfide catalyst copper chloride. When analyzed for the effect of exogenous reducing stress on biofilm-formation, both dsb mutants initially showed an escalated rdar morphotype development that later dissolved to reveal a smooth mucoid colony morphotype. From these results we conclude that biofilm-development in S. Typhimurium is affected by Periplasmic Protein disulphide bond status through CsgD, and discuss the involvement of selected GGDEF/EAL domain Protein(s) as signaling mediators.

  • modulation of biofilm formation in salmonella enterica serovar typhimurium by the Periplasmic dsba dsbb oxidoreductase system requires the ggdef eal domain Protein stm3615
    PLOS ONE, 2014
    Co-Authors: Naeem Anwar, Ute Römling, Syed Fazle Rouf, Mikael Rhen
    Abstract:

    In Salmonella enterica serovar Typhimurium (S. Typhimurium), biofilm-formation is controlled by the cytoplasmic intracellular small-molecular second messenger cyclic 3′, 5′-di- guanosine monophosphate (c-di-GMP) through the activities of GGDEF and EAL domain Proteins. Here we describe that deleting either dsbA or dsbB, respectively encoding a Periplasmic Protein disulfide oxidase and a cytoplasmic membrane disulfide oxidoreductase, resulted in increased biofilm-formation on solid medium. This increased biofilm-formation, defined as a red, dry and rough (rdar) colony morphotype, paralleled with enhanced expression of the biofilm master regulator CsgD and the biofilm-associated fimbrial subunit CsgA. Deleting csgD in either dsb mutant abrogated the enhanced biofilm-formation. Likewise, overexpression of the c-di-GMP phosphodiesterase YhjH, or mutationally inactivating the CsgD activator EAL-domain Protein YdiV, reduced biofilm-formation in either of the dsb mutants. Intriguingly, deleting the GGDEF-EAL domain Protein gene STM3615 (yhjK), previously not connected to rdar morphotype development, also abrogated the escalated rdar morphotype formation in dsb mutant backgrounds. Enhanced biofilm-formation in dsb mutants was furthermore annulled by exposure to the Protein disulfide catalyst copper chloride. When analyzed for the effect of exogenous reducing stress on biofilm-formation, both dsb mutants initially showed an escalated rdar morphotype development that later dissolved to reveal a smooth mucoid colony morphotype. From these results we conclude that biofilm-development in S. Typhimurium is affected by Periplasmic Protein disulphide bond status through CsgD, and discuss the involvement of selected GGDEF/EAL domain Protein(s) as signaling mediators.

Ben F Luisi - One of the best experts on this subject based on the ideXlab platform.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Hendrik W Van Veen, Ulrich Zachariae, Sjors H W Scheres, Ben F Luisi
    Abstract:

    The MacA–MacB–TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. Cryo-electron microscopy of the tripartite MacA–MacB–TolC multidrug transporter.

Ui Okada - One of the best experts on this subject based on the ideXlab platform.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Hendrik W Van Veen, Ulrich Zachariae, Sjors H W Scheres, Ben F Luisi
    Abstract:

    The MacA–MacB–TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. Cryo-electron microscopy of the tripartite MacA–MacB–TolC multidrug transporter.

  • structure of the macab tolc abc type tripartite multidrug efflux pump
    Nature microbiology, 2017
    Co-Authors: A W P Fitzpatrick, Hendrik W. Van Veen, Salome Llabres, Arthur Neuberger, James N Blaza, Ui Okada, Satoshi Murakami, Ulrich Zachariae, Xiao Chen Bai, Sjors H W Scheres
    Abstract:

    The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the Periplasmic Protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a Periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism.