[NMR paper] NMR Identification of the Binding Surfaces Involved in the Salmonella and Shigella Type III Secretion Tip-Translocon Protein-Protein Interactions.
Related ArticlesNMR Identification of the Binding Surfaces Involved in the Salmonella and Shigella Type III Secretion Tip-Translocon Protein-Protein Interactions.
Proteins. 2016 Apr 19;
Authors: McShan AC, Kaur K, Chatterjee S, Knight KM, De Guzman RN
Abstract
The type III secretion system (T3SS) is essential for the pathogenesis of many bacteria including Salmonella and Shigella, which together are responsible for millions of deaths worldwide each year. The structural component of the T3SS consists of the needle apparatus, which is assembled in part by the protein-protein interaction between the tip and the translocon. The atomic detail of the interaction between the tip and the translocon proteins is currently unknown. Here, we used NMR methods to identify that the N-terminal domain of the Salmonella SipB translocon protein interacts with the SipD tip protein at a surface at the distal region of the tip formed by the mixed ?/? domain and a portion of its coiled-coil domain. Likewise, the Shigella IpaB translocon protein and the IpaD tip protein interact with each other using similar surfaces identified for the Salmonella homologs. Furthermore, removal of the extreme N-terminal residues of the translocon protein, previously thought to be important for the interaction, had little change on the binding surface. Finally, mutations at the binding surface of SipD reduced invasion of Salmonella into human intestinal epithelial cells. Together, these results reveal the binding surfaces involved in the tip-translocon protein-protein interaction and advance our understanding of the assembly of the T3SS needle apparatus. This article is protected by copyright. All rights reserved.
PMID: 27093649 [PubMed - as supplied by publisher]
[NMR paper] NMR Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.
NMR Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.
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Biochemistry. 2015 Oct 9;
Authors: Chaudhury S, Nordhues BA, Kaur K, Zhang N, De Guzman RN
Abstract
Lung infection with Pseudomonas aeruginosa is the leading cause of death among cystic fibrosis patients. To initiate infection, P. aeruginosa assembles a protein nanomachine, the type III secretion...
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10-10-2015 06:47 PM
[NMR paper] High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.
High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.
High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.
Nat Commun. 2014;5:4976
Authors: Demers JP, Habenstein B, Loquet A, Kumar Vasa S, Giller K, Becker S, Baker D, Lange A, Sgourakis NG
Abstract
We introduce a general hybrid approach for determining the structures of supramolecular assemblies. Cryo-electron microscopy (cryo-EM) data define the overall...
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09-30-2014 02:18 PM
[NMR paper] NMR Model of PrgI-SipD Interaction and its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System.
NMR Model of PrgI-SipD Interaction and its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System.
Related Articles NMR Model of PrgI-SipD Interaction and its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System.
J Mol Biol. 2014 Jun 18;
Authors: Rathinavelan T, Lara-Tejero M, Lefebre M, Chatterjee S, McShan AC, Guo DC, Tang C, Galan JE, De Guzman RN
Abstract
Salmonella and other pathogenic bacteria use the type III secretion system (T3SS) to inject virulence proteins...
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06-22-2014 12:24 PM
[NMR paper] NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
Related Articles NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
J Biol Chem. 2004 Jul 23;279(30):31599-605
Authors: Xu XF, Tan YW, Lam L, Hackett J, Zhang M, Mok YK
The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only...
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[NMR paper] Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) che
Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate.
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J Am Chem Soc. 2002 Jan 23;124(3):372-3
Authors: Pintacuda G, Otting G
Gd-diethylenetriamine pentaacetic acid-bismethylamide, Gd(DTPA-BMA), is shown to be a reagent suitable for the identification of protein surfaces. Compared to the conventionally used spin-label TEMPOL, Gd(DTPA-BMA) is a stronger relaxation agent, requiring lesser concentrations...
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[NMR paper] NMR identification of protein surfaces using paramagnetic probes.
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Biochemistry. 1990 Oct 30;29(43):10041-8
Authors: Petros AM, Mueller L, Kopple KD
Paramagnetic agents produce line broadening and thus cancellation of anti phase cross-peak components in two-dimensional correlated nuclear magnetic resonance spectra. The specificity of this effect was examined to determine its utility for identifying surface residues of proteins. Ubiquitin and hen egg white...
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[NMR paper] NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
Eur J Biochem. 1999 Apr;261(2):562-8
Authors: Izadi-Pruneyre N, Wolff N, Redeker V, Wandersman C, Delepierre M, Lecroisey A
HasA is a haem-binding protein which is secreted under iron-deficiency conditions by the...
NMR Identification of the Binding Surfaces Involved in the Salmonella and Shigella Type III Secretion Tip-Translocon Protein-Protein Interactions.
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