Topology and organization of the Salmonella typhimurium type III secretion needle complex components.
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Topology and organization of the Salmonella typhimurium type III secretion needle complex components. / Schraidt, Oliver; Lefebre, Matthew D; Brunner, Matthias J; Schmied, Wolfgang H; Schmidt, Andreas; Radics, Julia; Mechtler, Karl; Galán, Jorge E; Marlovits, Thomas.
in: PLOS PATHOG, Jahrgang 6, Nr. 4, 4, 2010, S. 1000824.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Topology and organization of the Salmonella typhimurium type III secretion needle complex components.
AU - Schraidt, Oliver
AU - Lefebre, Matthew D
AU - Brunner, Matthias J
AU - Schmied, Wolfgang H
AU - Schmidt, Andreas
AU - Radics, Julia
AU - Mechtler, Karl
AU - Galán, Jorge E
AU - Marlovits, Thomas
PY - 2010
Y1 - 2010
N2 - The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.
AB - The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.
KW - Macromolecular Substances
KW - Cryoelectron Microscopy
KW - Bacterial Proteins/chemistry/ultrastructure
KW - Membrane Transport Proteins/chemistry/ultrastructure
KW - Salmonella typhimurium/chemistry/ultrastructure
KW - Macromolecular Substances
KW - Cryoelectron Microscopy
KW - Bacterial Proteins/chemistry/ultrastructure
KW - Membrane Transport Proteins/chemistry/ultrastructure
KW - Salmonella typhimurium/chemistry/ultrastructure
U2 - 10.1371/journal.ppat.1000824
DO - 10.1371/journal.ppat.1000824
M3 - SCORING: Journal article
VL - 6
SP - 1000824
JO - PLOS PATHOG
JF - PLOS PATHOG
SN - 1553-7366
IS - 4
M1 - 4
ER -