Three-dimensional model of Salmonella's needle complex at subnanometer resolution.
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Three-dimensional model of Salmonella's needle complex at subnanometer resolution. / Schraidt, Oliver; Marlovits, Thomas.
In: SCIENCE, Vol. 331, No. 6021, 6021, 2011, p. 1192-1195.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Three-dimensional model of Salmonella's needle complex at subnanometer resolution.
AU - Schraidt, Oliver
AU - Marlovits, Thomas
PY - 2011
Y1 - 2011
N2 - Type III secretion systems (T3SSs) are essential virulence factors used by many Gram-negative bacteria to inject proteins that make eukaryotic host cells accessible to invasion. The T3SS core structure, the needle complex (NC), is a ~3.5 megadalton-sized, oligomeric, membrane-embedded complex. Analyzing cryo-electron microscopy images of top views of NCs or NC substructures from Salmonella typhimurium revealed a 24-fold symmetry for the inner rings and a 15-fold symmetry for the outer rings, giving an overall C3 symmetry. Local refinement and averaging showed the organization of the central core and allowed us to reconstruct a subnanometer composite structure of the NC, which together with confident docking of atomic structures reveal insights into its overall organization and structural requirements during assembly.
AB - Type III secretion systems (T3SSs) are essential virulence factors used by many Gram-negative bacteria to inject proteins that make eukaryotic host cells accessible to invasion. The T3SS core structure, the needle complex (NC), is a ~3.5 megadalton-sized, oligomeric, membrane-embedded complex. Analyzing cryo-electron microscopy images of top views of NCs or NC substructures from Salmonella typhimurium revealed a 24-fold symmetry for the inner rings and a 15-fold symmetry for the outer rings, giving an overall C3 symmetry. Local refinement and averaging showed the organization of the central core and allowed us to reconstruct a subnanometer composite structure of the NC, which together with confident docking of atomic structures reveal insights into its overall organization and structural requirements during assembly.
KW - Mutation
KW - Image Processing, Computer-Assisted
KW - Models, Molecular
KW - Protein Structure, Tertiary
KW - Protein Conformation
KW - Crystallography, X-Ray
KW - Bacterial Secretion Systems
KW - Bacterial Proteins/chemistry/ultrastructure
KW - Cryoelectron Microscopy
KW - Membrane Proteins/chemistry/ultrastructure
KW - Membrane Transport Proteins/chemistry/ultrastructure
KW - Salmonella typhimurium/chemistry
KW - Mutation
KW - Image Processing, Computer-Assisted
KW - Models, Molecular
KW - Protein Structure, Tertiary
KW - Protein Conformation
KW - Crystallography, X-Ray
KW - Bacterial Secretion Systems
KW - Bacterial Proteins/chemistry/ultrastructure
KW - Cryoelectron Microscopy
KW - Membrane Proteins/chemistry/ultrastructure
KW - Membrane Transport Proteins/chemistry/ultrastructure
KW - Salmonella typhimurium/chemistry
M3 - SCORING: Journal article
VL - 331
SP - 1192
EP - 1195
JO - SCIENCE
JF - SCIENCE
SN - 0036-8075
IS - 6021
M1 - 6021
ER -
