ArticleJournal of biomolecular NMR2015
Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- The discovery and structural basis of two distinct state-dependent inhibitors of BamA.Nature communications · 2024Article
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- Detergent headgroups control TolC folding in vitro.Biophysical journal · 2023Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- Influence of Detergent and Lipid Composition on Reconstituted Membrane Proteins for Structural Studies.ACS omega · 2021Article
- Fake It 'Till You Make It-The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics.International journal of molecular sciences · 2020Review
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.Frontiers in molecular biosciences · 2019Article
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Preserved Transmembrane Segment Topology, Structure, and Dynamics in Disparate Micellar Environments.The journal of physical chemistry letters · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Flexibility in the Periplasmic Domain of BamA Is Important for Function.Structure (London, England : 1993) · 2017Article
- Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics.Angewandte Chemie (International ed. in English) · 2017Article
- Nanodiscs for structural and functional studies of membrane proteins.Nature structural & molecular biology · 2016Review
- NMR studies of membrane proteins.Journal of biomolecular NMR · 2015Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The insertase BamA is the central protein of the Bam complex responsible for outer membrane protein biogenesis in Gram-negative bacteria. BamA features a 16-stranded transmembrane β-barrel and five periplasmic POTRA domains, with a total molecular weight of 88 kDa. Whereas the structure of BamA has recently been determined by X-ray crystallography, its functional mechanism is not well understood. This mechanism comprises the insertion of substrates from a dynamic, chaperone-bound state into the bacterial outer membrane, and NMR spectroscopy is thus a method of choice for its elucidation. Here, we report solution NMR studies of different BamA constructs in three different membrane mimetic systems: LDAO micelles, DMPC:DiC7PC bicelles and MSP1D1:DMPC nanodiscs. The impact of biochemical parameters on the spectral quality was investigated, including the total protein concentration and the detergent:protein ratio. The barrel of BamA is folded in micelles, bicelles and nanodiscs, but the N-terminal POTRA5 domain is flexibly unfolded in the absence of POTRA4. Measurements of backbone dynamics show that the variable insertion region of BamA, located in the extracellular lid loop L6, features high local flexibility. Our work establishes biochemical preparation schemes for BamA, which will serve as a platform for structural and functional studies of BamA and its role within the Bam complex by solution NMR spectroscopy.
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