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 envelope of the assembly and rigid-body orientation of the subunits while solid-state nuclear magnetic resonance (ssNMR) chemical shifts and distance constraints define the local secondary structure, protein fold and inter-subunit interactions. Finally, Rosetta structure calculations provide a general framework to integrate the different sources of structural information. Combining a 7.7-Å cryo-EM density map and 996 ssNMR distance constraints, the structure of the type-III secretion system needle of Shigella flexneri is determined to a precision of 0.4 Å. The calculated structures are cross-validated using an independent data set of 691 ssNMR constraints and scanning transmission electron microscopy measurements. The hybrid model resolves the conformation of the non-conserved N terminus, which occupies a protrusion in the cryo-EM density, and reveals conserved pore residues forming a continuous pattern of electrostatic interactions, thereby suggesting a mechanism for effector protein translocation.
PMID: 25264107 [PubMed - as supplied by publisher]
[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...
nmrlearner
Journal club
0
06-22-2014 12:24 PM
[NMR images] Other methods are Cryo-EM(electron microscopy),
http://3.bp.blogspot.com/_H3VvAQred7I/SSRk1W97JBI/AAAAAAAAAII/G32vZntGdTE/s400/NMR.jpg
7/06/2014 7:13:57 PM GMT
Other methods are Cryo-EM(electron microscopy),
More...
nmrlearner
NMR pictures
0
06-07-2014 07:12 PM
[NMR paper] Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Phys Chem Chem Phys. 2013 Oct 21;15(39):16956-64
Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
The New York Structural Biology Center (NYSBC) seeks an experienced electron microscopist to join the staff of its Cryo-Electron Microscope Facility (http://cryoem.nysbc.org). The NYSBC is shared center that supports state-of-the-art research in cryo-EM, NMR, and X-ray. Cryo-EM facilities include four transmission electron microscopes and a new d...
More...
nmrlearner
Job marketplace
0
01-26-2011 04:21 AM
[NMR paper] Protein structure determination by high-resolution solid-state NMR spectroscopy: appl
Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.
Related Articles Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.
J Am Chem Soc. 2005 Jun 22;127(24):8618-26
Authors: Zech SG, Wand AJ, McDermott AE
High-resolution solid-state NMR spectroscopy has become a promising method for the determination of three-dimensional protein structures for systems which are difficult to crystallize or exhibit low...
High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.
Linear Mode
