NMR solution structure of the acylphosphatase from Escherichia coli

Katiuscia Pagano, Matteo Ramazzotti, Paolo Viglino, Gennaro Esposito, Donatella Degl'Innocenti, Niccolò Taddei, Alessandra Corazza

Research output: Contribution to journalArticle


The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by 1H and 15N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an α/β sandwich domain composed of four antiparallel and one parallel β-strand, assembled in a five-stranded β-sheet facing two antiparallel α-helices. The pairwise RMSD values calculated for the backbone atoms of E. coli and Sulfolobus solfataricus AcP, Bovine common type AcP and Horse muscle AcP are 2.18, 5.31 and 5.12 Å, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.

Original languageEnglish (US)
Pages (from-to)199-204
Number of pages6
JournalJournal of Biomolecular NMR
Issue number3
StatePublished - Nov 1 2006



  • Acylphosphatases
  • NMR structure

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

Cite this

Pagano, K., Ramazzotti, M., Viglino, P., Esposito, G., Degl'Innocenti, D., Taddei, N., & Corazza, A. (2006). NMR solution structure of the acylphosphatase from Escherichia coli. Journal of Biomolecular NMR, 36(3), 199-204. https://doi.org/10.1007/s10858-006-9073-2