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Staphylococcal nuclease and its complexes with nucleotidic inhibitors
Author(s) -
Cozzone Patrick J.,
Kaptein Robert
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80208-7
Subject(s) - nuclease , chemistry , calcium , binding site , enzyme , biochemistry , ternary complex , biophysics , biology , organic chemistry
A laser photo‐CIDNP study at 360 MHz of Staphylococcal nuclease shows that calcium binding induces a switch in the accessibility of Tyr 85 and Tyr 115 . This switch, which can be reverted by subsequent addition of pdTp inhibitor, might be relevant to the induction of nucleolytic activity upon calcium binding. The conformations of the ternary complexes of calcium (containing nuclease with pdTp, dTpCH 2 dTp and dTpCH 2 dTpCH 2 dT) are very similar and are interpreted in terms of comparable binding patterns at the active site of the enzyme.