Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

Ekaterina V. Filippova, Leigh A. Weston, Misty L. Kuhn, Brett Geissler, Alexandra M. Gehring, Nicola Armoush, Chinessa T. Adkins, George Minasov, Ievgeniia Dubrovska, Ludmilla Shuvalova, James R. Winsor, Luke D. Lavis, Karla J F Satchell, Daniel P. Becker, Wayne F. Anderson, R. Jeremy Johnson*

*Corresponding author for this work

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases.

Original languageEnglish (US)
Pages (from-to)10522-10535
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number15
DOIs
StatePublished - Apr 12 2013

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Filippova, E. V., Weston, L. A., Kuhn, M. L., Geissler, B., Gehring, A. M., Armoush, N., Adkins, C. T., Minasov, G., Dubrovska, I., Shuvalova, L., Winsor, J. R., Lavis, L. D., Satchell, K. J. F., Becker, D. P., Anderson, W. F., & Johnson, R. J. (2013). Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis. Journal of Biological Chemistry, 288(15), 10522-10535. https://doi.org/10.1074/jbc.M112.446625