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Crystal structure of FliM-SpeE complex from H. pylori
Structural highlights
FunctionSPEE_HELPY Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor.[1] Publication Abstract from PubMedThe 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 A resolution. SpeE dimer binds to FliM with micromolar binding affinity, and their interaction is mediated through the beta1' and beta2' 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. This article is protected by copyright. All rights reserved. A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori.,Zhang H, Lam KH, Lam WWL, Wong SYY, Chan VSF, Au SWN Mol Microbiol. 2017 Sep 4. doi: 10.1111/mmi.13829. PMID:28868744[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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