ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 51 citations in OpenAlex.
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- A key bacterial cytoskeletal cell division protein FtsZ as a novel therapeutic antibacterial drug target.Bosnian journal of basic medical sciences · 2020Review
- Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ.Biomolecules · 2020Article
- Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 inBiomolecules · 2020Article
- Revealing the Mechanisms of Synergistic Action of Two Magainin Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Solid-State NMR Investigations of the MHC II Transmembrane Domains: Topological Equilibria and Lipid Interactions.The Journal of membrane biology · 2019Article
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Structure, Topology, and Dynamics of Membrane-Inserted Polypeptides and Lipids by Solid-State NMR Spectroscopy: Investigations of the Transmembrane Domains of the DQ Beta-1 Subunit of the MHC II Receptor and of the COP I Protein p24.Frontiers in molecular biosciences · 2019Article
- Supramolecular Organization of Apolipoprotein-A-I-Derived Peptides within Disc-like Arrangements.Biophysical journal · 2018Article
- Bacterial Cell Division: Nonmodels Poised to Take the Spotlight.Annual review of microbiology · 2017Review
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- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- GdJournal of biomolecular NMR · 2017Article
- High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.Journal of biomolecular NMR · 2017Article
- HMGB1 Activates Proinflammatory Signaling via TLR5 Leading to Allodynia.Cell reports · 2016Article
Corrections and comments
- Erratum issuedCorrection for Das et al., Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.2015 · Rajagopalan, Malini R [corrected to Rajagopalan, Malini R]
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The 93-residue transmembrane protein CrgA in Mycobacterium tuberculosis is a central component of the divisome, a large macromolecular machine responsible for cell division. Through interactions with multiple other components including FtsZ, FtsQ, FtsI (PBPB), PBPA, and CwsA, CrgA facilitates the recruitment of the proteins essential for peptidoglycan synthesis to the divisome and stabilizes the divisome. CrgA is predicted to have two transmembrane helices. Here, the structure of CrgA was determined in a liquid-crystalline lipid bilayer environment by solid-state NMR spectroscopy. Oriented-sample data yielded orientational restraints, whereas magic-angle spinning data yielded interhelical distance restraints. These data define a complete structure for the transmembrane domain and provide rich information on the conformational ensembles of the partially disordered N-terminal region and interhelical loop. The structure of the transmembrane domain was refined using restrained molecular dynamics simulations in an all-atom representation of the same lipid bilayer environment as in the NMR samples. The two transmembrane helices form a left-handed packing arrangement with a crossing angle of 24° at the conserved Gly39 residue. This helix pair exposes other conserved glycine and alanine residues to the fatty acyl environment, which are potential sites for binding CrgA's partners such as CwsA and FtsQ. This approach combining oriented-sample and magic-angle spinning NMR spectroscopy in native-like lipid bilayers with restrained molecular dynamics simulations represents a powerful tool for structural characterization of not only isolated membrane proteins, but their complexes, such as those that form macromolecular machines.
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