Structural analysis of a prototypical ATPase from the type III secretion system (Q27643589)

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Brett Finlay

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object named as

B Brett Finlay

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author name string

Marija Vuckovic

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Wanyin Deng

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Natalie C J Strynadka

Nature Structural & Molecular Biology

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7

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publication date

February 2007

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published in

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volume

14

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issue

2

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page(s)

131-7

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cites work

Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events

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Structural and biochemical characterization of the type III secretion chaperones CesT and SigE

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Chaperone release and unfolding of substrates in type III secretion

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin

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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

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Substructure solution with SHELXD

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Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis

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From flagellum assembly to virulence: the extended family of type III export chaperones

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CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli.

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Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains

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Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization

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A pivotal role for reductive methylation in the de novo crystallization of a ternary complex composed of Yersinia pestis virulence factors YopN, SycN and YscB.

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The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH.

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Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases

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Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export

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Interactions among membrane and soluble components of the flagellar export apparatus of Salmonella

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Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly.

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Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of EnteropathogenicEscherichia coli

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Secretin of the enteropathogenic Escherichia coli type III secretion system requires components of the type III apparatus for assembly and localization

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Interactions among components of the Salmonella flagellar export apparatus and its substrates

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Type iii protein secretion in yersinia species

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Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.

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FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity.

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Protein modelling for all

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Regulation of type III secretion hierarchy of translocators and effectors in attaching and effacing bacterial pathogens

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Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis.

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The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer

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Process of protein transport by the type III secretion system

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YscN, the putative energizer of the Yersinia Yop secretion machinery

31 March 2020

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Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization

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Processing of X-ray diffraction data collected in oscillation mode

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The CCP4 suite: programs for protein crystallography

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NSMB1196

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

820430

1017121913

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820430

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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