Bacterial Pleckstrin Homology Domains: A Prokaryotic Origin for the PH Domain

Qingping Xu, Alex Bateman, Robert D. Finn, Polat Abdubek, Tamara Astakhova, Herbert L. Axelrod, Constantina Bakolitsa, Dennis Carlton, Connie Chen, Hsiu Ju Chiu, Michelle Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Kyle Ellrott, Dustin Ernst, Carol L. Farr, Julie Feuerhelm, Joanna C. GrantAnna Grzechnik, Gye Won Han, Lukasz Jaroszewski, Kevin K. Jin, Heath E. Klock, Mark W. Knuth, Piotr Kozbial, S. Sri Krishna, Abhinav Kumar, David Marciano, Daniel McMullan, Mitchell D. Miller, Andrew T. Morse, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Christina Puckett, Ron Reyes, Christopher L. Rife, Natasha Sefcovic, Henry J. Tien, Christine B. Trame, Henry van den Bedem, Dana Weekes, Tiffany Wooten, Keith O. Hodgson, John Wooley, Marc André Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

Pleckstrin homology (PH) domains have been identified only in eukaryotic proteins to date. We have determined crystal structures for three members of an uncharacterized protein family (Pfam PF08000), which provide compelling evidence for the existence of PH-like domains in bacteria (PHb). The first two structures contain a single PHb domain that forms a dome-shaped, oligomeric ring with C5 symmetry. The third structure has an additional helical hairpin attached at the C-terminus and forms a similar but much larger ring with C12 symmetry. Thus, both molecular assemblies exhibit rare, higher-order, cyclic symmetry but preserve a similar arrangement of their PHb domains, which gives rise to a conserved hydrophilic surface at the intersection of the β-strands of adjacent protomers that likely mediates protein-protein interactions. As a result of these structures, additional families of PHb domains were identified, suggesting that PH domains are much more widespread than originally anticipated. Thus, rather than being a eukaryotic innovation, the PH domain superfamily appears to have existed before prokaryotes and eukaryotes diverged.

Original languageEnglish (US)
Pages (from-to)31-46
Number of pages16
JournalJournal of molecular biology
Volume396
Issue number1
DOIs
StatePublished - Feb 12 2010

Keywords

  • Pleckstrin homology (PH) domain
  • bacterial PH domain (PHb)
  • higher-order symmetry
  • protein assembly
  • protein evolution

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Xu, Q., Bateman, A., Finn, R. D., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Carlton, D., Chen, C., Chiu, H. J., Chiu, M., Clayton, T., Das, D., Deller, M. C., Duan, L., Ellrott, K., Ernst, D., Farr, C. L., Feuerhelm, J., ... Wilson, I. A. (2010). Bacterial Pleckstrin Homology Domains: A Prokaryotic Origin for the PH Domain. Journal of molecular biology, 396(1), 31-46. https://doi.org/10.1016/j.jmb.2009.11.006