Investigations were performed on recombinant ribonuclease P2 from Sulfolobus solfataricus, previously cloned and expressed in Escherichia coli [Fusi, P., Grisa, M., Mombelli, E., Consonni, R., Tortora, P. and Vanoni, M. (1995) Gene 154, 99-103], MMR and photo-CIDNP spectroscopies showed that the enzyme possesses an aromatic cluster constisting of Phe(5), Tyr(7), Phe(31) and Tyr(33) while Trp(23) is fully exposed to solvent, Phe(31), Tyr(33) and Trp(23) located within a triple stranded antiparallel beta-sheet, each one being part of an amino acid stretch matching consensus sequences for RNA binding, Phe(31) and Trp(23) are exposed to and specifically interact with a flavin dye used as a model ligand, with a topology reminiscent of that found in several eubacterial and eukariotic RNA-binding proteins

Consonni, R., Limiroli, R., Molinari, H., Fusi, P., Grisa, M., Vanoni, M., et al. (1995). 1H-NMR and photo-CIDNP spectroscopies show a possible role for Trp23 and Phe31 in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus. FEBS LETTERS, 372(2-3), 135-139 [10.1016/0014-5793(95)00940-B].

1H-NMR and photo-CIDNP spectroscopies show a possible role for Trp23 and Phe31 in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus

FUSI, PAOLA ALESSANDRA;VANONI, MARCO ERCOLE;TORTORA, PAOLO
1995

Abstract

Investigations were performed on recombinant ribonuclease P2 from Sulfolobus solfataricus, previously cloned and expressed in Escherichia coli [Fusi, P., Grisa, M., Mombelli, E., Consonni, R., Tortora, P. and Vanoni, M. (1995) Gene 154, 99-103], MMR and photo-CIDNP spectroscopies showed that the enzyme possesses an aromatic cluster constisting of Phe(5), Tyr(7), Phe(31) and Tyr(33) while Trp(23) is fully exposed to solvent, Phe(31), Tyr(33) and Trp(23) located within a triple stranded antiparallel beta-sheet, each one being part of an amino acid stretch matching consensus sequences for RNA binding, Phe(31) and Trp(23) are exposed to and specifically interact with a flavin dye used as a model ligand, with a topology reminiscent of that found in several eubacterial and eukariotic RNA-binding proteins
Articolo in rivista - Articolo scientifico
NMR, ribonuclease, S. solfataricus
English
135
139
5
Consonni, R., Limiroli, R., Molinari, H., Fusi, P., Grisa, M., Vanoni, M., et al. (1995). 1H-NMR and photo-CIDNP spectroscopies show a possible role for Trp23 and Phe31 in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus. FEBS LETTERS, 372(2-3), 135-139 [10.1016/0014-5793(95)00940-B].
Consonni, R; Limiroli, R; Molinari, H; Fusi, P; Grisa, M; Vanoni, M; Tortora, P
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/15677
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