Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
J Struct Biol. 2017 Nov 29;:
Authors: Pinto C, Mance D, Julien M, Daniels M, Weingarth M, Baldus M
Abstract
Significant progress has been made in obtaining a structural insight into the assembly of the ?-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane mimetic and revealed structural variations in the central domain, BamA, as well as the lipoprotein BamC. We have used cellular solid-state NMR spectroscopy to examine the entire BamABCDE complex in native outer membranes and obtained data on the BamCDE subcomplex in outer membranes, in addition to synthetic bilayers. To reduce spectral crowding, we utilized proton-detected experiments and employed amino-acid specific isotope-labelling in (13C, 13C) correlation experiments. Taken together, the results provide insight into the overall fold and assembly of the BAM complex in native membranes, in particular regarding the structural flexibility of BamC in the absence of the core unit BamA.
PMID: 29197585 [PubMed - as supplied by publisher]
[NMR paper] Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
In nature, proteins are organized into highly ordered self-assembled structures with various morphologies and dimensions. In their Communication (DOI: 10.1002/anie.201703052), Y. Ma, G. Chen, and co-workers report the fabrication of protein assemblies by using native protein LecA as a building block through sugar–protein interactions and rhodamine dimerization. The morphologies and dimensions of the protein assemblies can be controlled by the length...
Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy
Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy
Abstract
Membrane proteins play many critical roles in cells, mediating flow of material and information across cell membranes. They have evolved to perform these functions in the environment of a cell membrane, whose physicochemical properties are often different from those of common cell membrane mimetics used for structure determination. As a result, membrane proteins are difficult to study by traditional methods of structural biology, and they are significantly underrepresented in the protein...
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N. Santiago-Miranda, Gary J. Pielak and Fang Tian
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja204062v/aop/images/medium/ja-2011-04062v_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja204062v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/BuOPwKpaHdw
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07-27-2011 11:24 AM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
J Am Chem Soc. 2011 Jul 21;
Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F
The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...
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07-23-2011 08:54 AM
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Top Curr Chem. 2011 May 20;
Authors: Koch K, Afonin S, Ieronimo M, Berditsch M, Ulrich AS
To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR,...
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05-21-2011 07:51 PM
Ph.D. student in solid-state NMR: Studying protein folding and assembly at atomic sca
Ph.D. student in solid-state NMR: Studying protein folding and assembly at atomic scale
Description of the Faculty / Research group
The Faculty of Science consists of six departments: Biology, Pharmaceutical Sciences, Information and Computing Sciences, Physics and Astronomy, Mathematics and Chemistry. The Faculty is home to 3500 students and nearly 2000 staff and is internationally renowned for the quality of its research.
The NMR Research Group is part of the Chemistry Department (Universiteit Utrecht fac. Scheikunde) and belongs to the Bijvoet Center for Biomolecular...
Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
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