4rz3

Crystal structure of the MinD-like ATPase FlhG

spinqualitylabelsall models 4rz3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rz3 is a 2 chain structure with sequence from Geobacillus thermodenitrificans NG80-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: ADP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4IMB4_GEOTN Publication Abstract from PubMed The number and location of flagella, bacterial organelles of locomotion, are species specific and appear in regular patterns that represent one of the earliest taxonomic criteria in microbiology. However, the mechanisms that reproducibly establish these patterns during each round of cell division are poorly understood. FlhG (previously YlxH) is a major determinant for a variety of flagellation patterns. Here, we show that FlhG is a structural homolog of the ATPase MinD, which serves in cell-division site determination. Like MinD, FlhG forms homodimers that are dependent on ATP and lipids. It interacts with a complex of the flagellar C-ring proteins FliM and FliY (also FliN) in the Gram-positive, peritrichous-flagellated Bacillus subtilis and the Gram-negative, polar-flagellated Shewanella putrefaciens. FlhG interacts with FliM/FliY in a nucleotide-independent manner and activates FliM/FliY to assemble with the C-ring protein FliG in vitro. FlhG-driven assembly of the FliM/FliY/FliG complex is strongly enhanced by ATP and lipids. The protein shows a highly dynamic subcellular distribution between cytoplasm and flagellar basal bodies, suggesting that FlhG effects flagellar location and number during assembly of the C-ring. We describe the molecular evolution of a MinD-like ATPase into a flagellation pattern effector and suggest that the underappreciated structural diversity of the C-ring proteins might contribute to the formation of different flagellation patterns. MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.,Schuhmacher JS, Rossmann F, Dempwolff F, Knauer C, Altegoer F, Steinchen W, Dorrich AK, Klingl A, Stephan M, Linne U, Thormann KM, Bange G Proc Natl Acad Sci U S A. 2015 Mar 10;112(10):3092-7. doi:, 10.1073/pnas.1419388112. Epub 2015 Mar 2. PMID:25733861 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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