ArticleThe Journal of biological chemistry2015
Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the β-barrel assembly machine.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 55 citations in OpenAlex.
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural characterization of the POTRA domains from A. baumannii reveals new conformations in BamA.Structure (London, England : 1993) · 2024Article
- Thanatin: A Promising Antimicrobial Peptide Targeting the Achilles' Heel of Multidrug-Resistant Bacteria.International journal of molecular sciences · 2024Review
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- The TAM, a Translocation and Assembly Module for protein assembly and potential conduit for phospholipid transfer.EMBO reports · 2024Review
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Dissecting the Organization of a β-Barrel Assembly Machinery (BAM) Complex by Neutron Reflectometry.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- Surface-tethered planar membranes containing the β-barrel assembly machinery: a platform for investigating bacterial outer membrane protein folding.Biophysical journal · 2021Article
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- OMPdb: A Global Hub of Beta-Barrel Outer Membrane Proteins.Frontiers in bioinformatics · 2021Article
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- Identification of a Compound That Inhibits the Growth of Gram-Negative Bacteria by Blocking BamA-BamD Interaction.Frontiers in microbiology · 2020Article
- Countering Gram-Negative Antibiotic Resistance: Recent Progress in Disrupting the Outer Membrane with Novel Therapeutics.Antibiotics (Basel, Switzerland) · 2019Review
- Outer Membrane Protein Insertion by the β-barrel Assembly Machine.EcoSal Plus · 2019Review
- Structural and functional insights into the role of BamD and BamE within the β-barrel assembly machinery inThe Journal of biological chemistry · 2018Article
- Folding of a bacterial integral outer membrane protein is initiated in the periplasm.Nature communications · 2017Article
- Outer Membrane Biogenesis.Annual review of microbiology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The β-barrel assembly machinery (BAM) mediates folding and insertion of β-barrel outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria. BAM is a five-protein complex consisting of the β-barrel OMP BamA and lipoproteins BamB, -C, -D, and -E. High resolution structures of all the individual BAM subunits and a BamD-BamC complex have been determined. However, the overall complex architecture remains elusive. BamA is the central component of BAM and consists of a membrane-embedded β-barrel and a periplasmic domain with five polypeptide translocation-associated (POTRA) motifs thought to interact with the accessory lipoproteins. Here we report the crystal structure of a fusion between BamB and a POTRA3-5 fragment of BamA. Extended loops 13 and 17 protruding from one end of the BamB β-propeller contact the face of the POTRA3 β-sheet in BamA. The interface is stabilized by several hydrophobic contacts, a network of hydrogen bonds, and a cation-π interaction between BamA Tyr-255 and BamB Arg-195. Disruption of BamA-BamB binding by BamA Y255A and probing of the interface by disulfide bond cross-linking validate the physiological relevance of the observed interface. Furthermore, the structure is consistent with previously published mutagenesis studies. The periplasmic five-POTRA domain of BamA is flexible in solution due to hinge motions in the POTRA2-3 linker. Modeling BamB in complex with full-length BamA shows BamB binding at the POTRA2-3 hinge, suggesting a role in modulation of BamA flexibility and the conformational changes associated with OMP folding and insertion.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.