ArticleJournal of biomolecular NMR2015
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
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 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.Nature communications · 2021Article
- Surface-tethered planar membranes containing the β-barrel assembly machinery: a platform for investigating bacterial outer membrane protein folding.Biophysical journal · 2021Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR.Nature communications · 2018Article
- Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Flexibility in the Periplasmic Domain of BamA Is Important for Function.Structure (London, England : 1993) · 2017Article
- Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Structure (London, England : 1993) · 2016Review
- Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy.Biophysical journal · 2016Article
- Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.Journal of biomolecular NMR · 2016Article
- Efficient cellular solid-state NMR of membrane proteins by targeted protein labeling.Journal of biomolecular NMR · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The β-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly understood. With its 790 residues, BamA presents a challenge to current NMR methods. We utilized a "divide and conquer" approach in which we first obtained resonance assignments for BamA's periplasmic POTRA domains 4 and 5 by solution NMR. Comparison of these assignments to solid-state NMR (ssNMR) data obtained on two BamA constructs including the transmembrane domain and one or two soluble POTRA domains suggested that the fold of POTRA domain 5 critically depends on the interface with POTRA 4. Using specific labeling schemes we furthermore obtained ssNMR resonance assignments for residues in the extracellular loop 6 that is known to be crucial for BamA-mediated substrate folding and insertion. Taken together, our data provide novel insights into the conformational stability of membrane-embedded, non-crystalline BamA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.