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

Abstract

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
Volume36
Issue number3
DOIs
StatePublished - Nov 1 2006

Fingerprint

Escherichia coli
Nuclear magnetic resonance
Catalytic Domain
Sulfolobus solfataricus
Horses
Muscle
Hydrolysis
Muscles
Atoms
Enzymes
acylphosphatase
Proton Magnetic Resonance Spectroscopy

Keywords

  • Acylphosphatases
  • NMR structure

ASJC Scopus subject areas

  • Spectroscopy
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

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

NMR solution structure of the acylphosphatase from Escherichia coli. / Pagano, Katiuscia; Ramazzotti, Matteo; Viglino, Paolo; Esposito, Gennaro; Degl'Innocenti, Donatella; Taddei, Niccolò; Corazza, Alessandra.

In: Journal of Biomolecular NMR, Vol. 36, No. 3, 01.11.2006, p. 199-204.

Research output: Contribution to journalArticle

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, vol. 36, no. 3, pp. 199-204. https://doi.org/10.1007/s10858-006-9073-2
Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N et al. NMR solution structure of the acylphosphatase from Escherichia coli. Journal of Biomolecular NMR. 2006 Nov 1;36(3):199-204. https://doi.org/10.1007/s10858-006-9073-2
Pagano, Katiuscia ; Ramazzotti, Matteo ; Viglino, Paolo ; Esposito, Gennaro ; Degl'Innocenti, Donatella ; Taddei, Niccolò ; Corazza, Alessandra. / NMR solution structure of the acylphosphatase from Escherichia coli. In: Journal of Biomolecular NMR. 2006 ; Vol. 36, No. 3. pp. 199-204.
@article{a931da98403d463eaefdb8401e1ea2bb,
title = "NMR solution structure of the acylphosphatase from Escherichia coli",
abstract = "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 {\AA}, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.",
keywords = "Acylphosphatases, NMR structure",
author = "Katiuscia Pagano and Matteo Ramazzotti and Paolo Viglino and Gennaro Esposito and Donatella Degl'Innocenti and Niccol{\`o} Taddei and Alessandra Corazza",
year = "2006",
month = "11",
day = "1",
doi = "10.1007/s10858-006-9073-2",
language = "English (US)",
volume = "36",
pages = "199--204",
journal = "Journal of Biomolecular NMR",
issn = "0925-2738",
publisher = "Springer Netherlands",
number = "3",

}

TY - JOUR

T1 - NMR solution structure of the acylphosphatase from Escherichia coli

AU - Pagano, Katiuscia

AU - Ramazzotti, Matteo

AU - Viglino, Paolo

AU - Esposito, Gennaro

AU - Degl'Innocenti, Donatella

AU - Taddei, Niccolò

AU - Corazza, Alessandra

PY - 2006/11/1

Y1 - 2006/11/1

N2 - 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.

AB - 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.

KW - Acylphosphatases

KW - NMR structure

UR - http://www.scopus.com/inward/record.url?scp=33751002965&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33751002965&partnerID=8YFLogxK

U2 - 10.1007/s10858-006-9073-2

DO - 10.1007/s10858-006-9073-2

M3 - Article

VL - 36

SP - 199

EP - 204

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

SN - 0925-2738

IS - 3

ER -