NMR solution structure of the acylphosphatase from Escherichia coli.
The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-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 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.
Pagano
Katiuscia
K
Department of Biomedical Sciences and Technologies, University of Udine, Udine, Italy.
Ramazzotti
Matteo
M
Viglino
Paolo
P
Esposito
Gennaro
G
Degl'Innocenti
Donatella
D
Taddei
Niccolò
N
Corazza
Alessandra
A
D017766:Acid Anhydride Hydrolases / Q000737:chemistry*; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D016415:Sequence Alignment; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000097024:Acylphosphatase