4RZ2

Crystal structure of the MinD-like ATPase FlhG

Summary for 4RZ2

• Entry DOI: 10.2210/pdb4rz2/pdb
• Related: 3SYN 4RZ3
• Descriptor: Site-determining protein (2 entities in total)
• Functional Keywords: p-loop, walker a, simibi, flagellum, cell division, structural protein
• Biological source: Geobacillus thermodenitrificans
• Total number of polymer chains: 2
• Total formula weight: 65320.91

Authors

Schuhmacher, J.S.,Bange, G. (deposition date: 2014-12-18, release date: 2015-03-04, Last modification date: 2023-09-20)

Primary citation

Schuhmacher, J.S.,Rossmann, F.,Dempwolff, F.,Knauer, C.,Altegoer, F.,Steinchen, W.,Dorrich, A.K.,Klingl, A.,Stephan, M.,Linne, U.,Thormann, K.M.,Bange, G.
MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.
Proc.Natl.Acad.Sci.USA, 112:3092-3097, 2015

PubMed Abstract: 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.

PubMed: 25733861
DOI: 10.1073/pnas.1419388112

Experimental method

X-RAY DIFFRACTION (2.8 Å)