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TitleLarge scale structural rearrangement of a serine hydrolase from Francisella tularensis facilitates catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 10522-10535, Year 2013
Publish dateMay 7, 2012 (structure data deposition date)
AuthorsFilippova, E.V. / Weston, L.A. / Kuhn, M.L. / Geissler, B. / Gehring, A.M. / Armoush, N. / Adkins, C.T. / Minasov, G. / Dubrovska, I. / Shuvalova, L. ...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. / Becker, D.P. / Anderson, W.F. / Johnson, R.J.
External linksJ. Biol. Chem. / PubMed:23430251
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-4f21:
Crystal structure of carboxylesterase/phospholipase family protein from Francisella tularensis
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-0S1:
N-((1R,2S)-2-allyl-4-oxocyclobutyl)-4-methylbenzenesulfonamide, bound form

ChemComp-HOH:
WATER

Source
  • francisella tularensis subsp. tularensis (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Structural Genomics / NIAID / National Institute of Allergy and Infectious Diseases / Center for Structural Genomics of Infectious Diseases / CSGID / carboxylesterase / phospholipase / HYDROLASE-HYDROLASE INHIBITOR complex

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