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Thermodynamics of nucleotide binding to NBS-I of the Bacillus subtilis preprotein translocase subunit SecA.
den Blaauwen, T; van der Wolk, J P; van der Does, C; van Wely, K H; Driessen, A J.
Afiliação
  • den Blaauwen T; Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.
FEBS Lett ; 458(2): 145-50, 1999 Sep 17.
Article em En | MEDLINE | ID: mdl-10481054
SecA is the dissociatable nucleotide and preprotein binding subunit of the bacterial translocase. The thermodynamics of nucleotide binding to soluble SecA at nucleotide binding site I were determined by isothermal titration calorimetry. Binding of ADP and non-hydrolyzable ATPgammaS is enthalpy-driven (DeltaH(0) of -14.44 and -5.56 kcal/mol, respectively), but is accompanied by opposite entropic contributions (DeltaS(0) of -18.25 and 9.55 cal/mol/K, respectively). ADP binding results in a large change in the heat capacity of SecA (DeltaC(p)=-780 cal/mol/K). It is suggested that ADP binding promotes the interaction between the two thermodynamically discernible domains of SecA which is accompanied by a shielding of hydrophobic surface from solvent.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Proteínas de Membrana Transportadoras / Bacillus subtilis / Proteínas de Bactérias / Difosfato de Adenosina / Trifosfato de Adenosina / Adenosina Trifosfatases / Proteínas de Escherichia coli / Precursores Enzimáticos Idioma: En Ano de publicação: 1999 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Proteínas de Membrana Transportadoras / Bacillus subtilis / Proteínas de Bactérias / Difosfato de Adenosina / Trifosfato de Adenosina / Adenosina Trifosfatases / Proteínas de Escherichia coli / Precursores Enzimáticos Idioma: En Ano de publicação: 1999 Tipo de documento: Article