5X0Z

Crystal structure of FliM-SpeE complex from H. pylori

Summary for 5X0Z

• Entry DOI: 10.2210/pdb5x0z/pdb
• Descriptor: Polyamine aminopropyltransferase, Flagellar motor switch protein (FliM), CITRATE ANION, ... (4 entities in total)
• Functional Keywords: flagellar motor, h. pylori, motility, transferase-motor protein complex, transferase/motor protein
• Biological source: Helicobacter pylori 26695; More
• Cellular location: Cytoplasm : O25503
• Total number of polymer chains: 6
• Total formula weight: 167257.55

Authors

Zhang, H.,Au, S.W.N. (deposition date: 2017-01-23, release date: 2017-09-13, Last modification date: 2023-11-22)

Primary citation

Zhang, H.,Lam, K.H.,Lam, W.W.L.,Wong, S.Y.Y.,Chan, V.S.F.,Au, S.W.N.
A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori
Mol. Microbiol., 106:690-703, 2017

PubMed Abstract: The flagellar motor is an important virulence factor in infection by many bacterial pathogens. Motor function can be modulated by chemotactic proteins and recently appreciated proteins that are not part of the flagellar or chemotaxis systems. How these latter proteins affect flagellar activity is not fully understood. Here, we identified spermidine synthase SpeE as an interacting partner of switch protein FliM in Helicobacter pylori using pull-down assay and mass spectrometry. To understand how SpeE contributes to flagellar motility, a speE-null mutant was generated and its motility behavior was evaluated. We found that deletion of SpeE did not affect flagellar formation, but induced clockwise rotation bias. We further determined the crystal structure of the FliM-SpeE complex at 2.7 Å resolution. SpeE dimer binds to FliM with micromolar binding affinity, and their interaction is mediated through the β1' and β2' region of FliM middle domain. The FliM-SpeE binding interface partially overlaps with the FliM surface that interacts with FliG and is essential for proper flagellar rotational switching. By a combination of protein sequence conservation analysis and pull-down assays using FliM and SpeE orthologues in E. coli, our data suggest that FliM-SpeE association is unique to Helicobacter species.

PubMed: 28868744
DOI: 10.1111/mmi.13829

Experimental method

X-RAY DIFFRACTION (2.7 Å)