http://www.cnr.it/ontology/cnr/individuo/prodotto/ID54152
Investigations of Sso7d Catalytic Residues by NMR Titration Shifts and Electrostatic Calculations (Articolo in rivista)
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- Label
- Investigations of Sso7d Catalytic Residues by NMR Titration Shifts and Electrostatic Calculations (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/bi0265168 (literal)
- Alternative label
Consonni R., Arosio I., Belloni B., Fogolari F., Fusi P., Shehi E., Zetta L. (2003)
Investigations of Sso7d Catalytic Residues by NMR Titration Shifts and Electrostatic Calculations
in Biochemistry (Easton)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Consonni R., Arosio I., Belloni B., Fogolari F., Fusi P., Shehi E., Zetta L. (literal)
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- http://pubs.acs.org/doi/abs/10.1021/bi0265168 (literal)
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- Articolo in pubblicazione internazionale (literal)
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- Consonni R., Arosio I., Belloni B.,Zetta L. Istituo per lo studio delle Macromolecole, CNR Milano
Fusi P., Shehi E., Dip. Di Biotecnologie e Bioscienze, Univ. Milano
Fogolari F., Dip. Scientifico e Tecnologico, Univ. Verona (literal)
- Titolo
- Investigations of Sso7d Catalytic Residues by NMR Titration Shifts and Electrostatic Calculations (literal)
- Abstract
- Sso7d is a small basic protein consisting of 62 amino acids isolated from the thermoacidophilic
archeobacterium Sulfolobus solfataricus. The protein is endowed with DNA binding properties, RNase
activity, and the capability of rescuing aggregated proteins in the presence of ATP. In this study, the
electrostatic properties of Sso7d are investigated by using the Poisson-Boltzmann calculation of the surface
potential distribution and following by NMR spectroscopy the proton chemical shift pH titration of acidic
residues. Although the details of the catalytic mechanism still have to be defined, the results from NMR
experiments confirm the possible involvement of Glu35 as the proton acceptor in the catalytic reaction,
as seen by its abnormally high pKa value. Poisson-Boltzmann calculations and NMR titration shifts suggest
the presence of a possible hydrogen bond between Glu35 and Tyr33, with a consequent rather rigid
arrangement at these positions. Comparison with RNase T1 suggests that Tyr7 may be a good candidate
for acting as a proton donor in the active site of Sso7d as shown by its low phenolic pKa of 9.3. Titration
experiments performed with the UpA, a RNA dinucleotide model, showed that the protein residues affected
by the interaction are mainly located in a different region with respect to the surface affected by DNA
recognition, in good agreement with the surface potential distribution found with electrostatic calculations. (literal)
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