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Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor.

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Kang GB, Song HE, Kim MK, Youn HS, Lee JG, An JY, Chun JS, Jeon H, Eom SH
OpenAccess logo Mol Microbiol 76 1222-31 (2010)
Cited: 17 times
EuropePMC logo PMID: 20398219

Abstract

In Gram-negative bacteria, proper placement of the FtsZ ring, mediated by nucleoid occlusion and the activities of the dynamic oscillating Min proteins MinC, MinD and MinE, is required for correct positioning of the cell division septum. MinE is a topological specificity factor that counters the activity of MinCD division inhibitor at the mid-cell division site. Its structure consists of an anti-MinCD domain and a topology specificity domain (TSD). Previous NMR analysis of truncated Escherichia coli MinE showed that the TSD domain contains a long alpha-helix and two anti-parallel beta-strands, which mediate formation of a homodimeric alpha/beta structure. Here we report the crystal structure of full-length Helicobacter pylori MinE and redefine its TSD based on that structure. The N-terminal region of the TSD (residues 19-26), previously defined as part of the anti-MinCD domain, forms a beta-strand (betaA) and participates in TSD folding. In addition, H. pylori MinE forms a dimer through the interaction of anti-parallel betaA-strands. Moreover, we observed serial dimer-dimer interactions within the crystal packing, resulting in the formation of a multimeric structure. We therefore redefine the functional domain of MinE and propose that a multimeric filamentous structure is formed through anti-parallel beta-strand interactions.

Articles - 3ku7 mentioned but not cited (1)

  1. Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor. Kang GB, Song HE, Kim MK, Youn HS, Lee JG, An JY, Chun JS, Jeon H, Eom SH. Mol Microbiol 76 1222-1231 (2010)


Reviews citing this publication (4)

  1. Unusual biophysics of intrinsically disordered proteins. Uversky VN. Biochim Biophys Acta 1834 932-951 (2013)
  2. Spatial control of the cell division site by the Min system in Escherichia coli. Shih YL, Zheng M. Environ Microbiol 15 3229-3239 (2013)
  3. Toward Spatially Regulated Division of Protocells: Insights into the E. coli Min System from in Vitro Studies. Kretschmer S, Schwille P. Life (Basel) 4 915-928 (2014)
  4. Mechanistic insights of the Min oscillator via cell-free reconstitution and imaging. Mizuuchi K, Vecchiarelli AG. Phys Biol 15 031001 (2018)

Articles citing this publication (12)

  1. The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis. Park KT, Wu W, Battaile KP, Lovell S, Holyoak T, Lutkenhaus J. Cell 146 396-407 (2011)
  2. Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Wu W, Park KT, Holyoak T, Lutkenhaus J. Mol Microbiol 79 1515-1528 (2011)
  3. Protein self-organization: lessons from the min system. Loose M, Kruse K, Schwille P. Annu Rev Biophys 40 315-336 (2011)
  4. The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature. Shih YL, Huang KF, Lai HM, Liao JH, Lee CS, Chang CM, Mak HM, Hsieh CW, Lin CC. PLoS One 6 e21425 (2011)
  5. Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE. Ghasriani H, Ducat T, Hart CT, Hafizi F, Chang N, Al-Baldawi A, Ayed SH, Lundström P, Dillon JA, Goto NK. Proc Natl Acad Sci U S A 107 18416-18421 (2010)
  6. Acid-regulated gene expression of Helicobacter pylori: Insight into acid protection and gastric colonization. Marcus EA, Sachs G, Scott DR. Helicobacter 23 e12490 (2018)
  7. Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system. Zheng M, Chiang YL, Lee HL, Kong LR, Hsu ST, Hwang IS, Rothfield LI, Shih YL. J Biol Chem 289 21252-21266 (2014)
  8. MinC/MinD copolymers are not required for Min function. Park KT, Du S, Lutkenhaus J. Mol Microbiol 98 895-909 (2015)
  9. Molecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing Escherichia coli Cells. Walsh JC, Angstmann CN, Duggin IG, Curmi PM. PLoS One 10 e0128148 (2015)
  10. Regulation of symmetric bacterial cell division by MinE: What is the role of conformational dynamics? Ghasriani H, Goto NK. Commun Integr Biol 4 101-103 (2011)
  11. Intrinsic characteristics of Min proteins on the cell division of Helicobacter pylori. Nishida Y, Takeuchi H, Morimoto N, Umeda A, Kadota Y, Kira M, Okazaki A, Matsumura Y, Sugiura T. FEMS Microbiol Lett 363 fnw025 (2016)
  12. Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli. Walsh JC, Angstmann CN, Duggin IG, Curmi PMG. PLoS One 12 e0185947 (2017)


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