2mmu

Structure of CrgA, a Cell Division Structural and Regulatory Protein from Mycobacterium tuberculosis, in Lipid Bilayers

spinqualitylabelsall models 2mmu, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mmu is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CRGA_MYCTU] Involved in cell division. Plays an important role in septal peptidoglycan synthesis and cell shape morphogenesis. May facilitate the recruitment of the peptidoglycan synthesis machinery to poles and septal zones and coordinate peptidoglycan synthesis at these sites.[HAMAP-Rule:MF_00631] Publication Abstract from PubMed 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 degrees 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. Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.,Das N, Dai J, Hung I, Rajagopalan MR, Zhou HX, Cross TA Proc Natl Acad Sci U S A. 2015 Jan 13;112(2):E119-26. doi:, 10.1073/pnas.1415908112. Epub 2014 Dec 29. PMID:25548160 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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