Topography of the Active Site of Staphylococcal Nuclease
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چکیده
منابع مشابه
The active site of staphylococcal nuclease: paramagnetic relaxation of bound nucleotide inhibitor nuclei by lanthanide ions.
The structure of 3',5'-thymidine diphosphate bound in the active site of staphylococcal nuclease (EC 3.1.4.7) was studied by measuring the relaxation rate enhancement of substrate analog nuclei by a paramagnetic metal ion. The lanthanide ion, Gd(III), was substituted for Ca(II) in the formation of the ternary complex of nuclease-Gd(III)-3',5'-thymidine diphosphate. Measurements were made of the...
متن کاملCross-linking of aminotyrosyl residues in the active site of staphylococcal nuclease.
Derivatives of staphylococcal nuclease containing monoaminotyrosyl residues in position 85 or 115 were treated at pH 5 with two bifunctional reagents, p,p’-difkoro-m,m’dinitrodiphenylsulfone (F2DPS) and 1,5-difluoro-2,4-dinitrobenzene (F*DNB). Monofunctional reaction occurred exclusively at the aminotyrosyl residue, and there was no significant hydrolysis of the second fluorine atom. The excess...
متن کاملNuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments.
An extracellular nuclease produced by Staphylococcus aureus1-3 has been shown to contain 149 amino acid residues (mol wt, 16,807) and to lack both sulfhydryl groups and disulfide bonds (Fig. 1).3-5 The enzyme catalyzes the cleavage of both DNA and RNA to yield 3’-nucleotides.2s 3 The absolute requirement for Ca++ l* 2s 6 may be explained by the interdependency of Gaff and nucleotide binding to ...
متن کامل[Cold denaturation of staphylococcal nuclease].
It has been shown that the structure of staphylococcal nuclease breaks down reversibly both at a temperature increase above 20 degrees C and at its decrease. Both the heat and cold denaturations of protein are well approximated by a transition between two states differing in heat capacity, which means that the whole protein molecule represents a unique cooperative system with a well developed h...
متن کاملUltrafast solvation dynamics at internal site of staphylococcal nuclease investigated by site-directed mutagenesis
Solvation is essential for protein activities. To study internal solvation of protein, site-directed mutagenesis is applied. Intrinsic fluorescent probe, tryptophan, is inserted into desired position inside protein molecule for ultrafast spectroscopic study. Here we review this unique method for protein dynamics researches. We introduce the frontiers of protein solvation, site-directed mutagene...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63371-x