ATP hydrolysis is essential for the function of the Uup ATP-binding cassette ATPase in precise excision of transposons. J Biol Chem. 2006; 281 :6850–6859. [ PubMed ]Murat D, Bance P, Callebaut I, Dassa E (2006) ATP hydrolysis is essential for the function of the Uup ATP-binding ...
states of MutS as reflected in: (i) a specific and highly stable MutS–mismatch complex in the absence of a nucleotide; (ii) a specific but less stable complex in the presence of ATP hydrolysis; and (iii) an irreversibly dissociated complex in the presence of ATP binding (ATPγS). Such...
The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control the folding and activation of several client proteins in the eukaryotic cell. To elucidate how the local ATPase reaction in the active si
Analysis of Walker motif B mutants suggests that ATP hydrolysis at the two ABC domains is strictly coordinated and is essential for the function of Uup in vivo. 展开 关键词: Hydrolysis Essential Function ATPbinding Cassette Excision Transposons ...
Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysis of ATP, which drives a molecular clamp via transient dimerization of the N-terminal domains. The crystal structure of the middle segment of yeast Hsp90 reveals considerable evolutionary divergence ...
of enzymes, motor proteins, and transport proteins to carry out the work of the cell. Also, the hydrolysis yields free inorganic phosphate and adenosine diphosphate, which can be broken down further to another phosphate ion and adenosine monophosphate. ATP can also be broken down to adenosine ...
The biosynthesis of peptides involves aminoacyl adenylates (aa-AMPs), formed through the reaction of ATP with α-amino acids (aas) (Fig. 1), that are subsequently used to aminoacylate tRNA. Their standard free energy of hydrolysis value ΔG°′ =ca. −70 kJ mol−1, determined for...
The chemical mechanism of ATP hydrolysis by nitrogenase is discussed in terms of results from isotopic exchange studies using [18O4]-Pi, b,g-[18O]-ATP, and g-[18O4]-ATP as probes of reversibility (ATP = ADP + Pi) and of the freedom of rotation around the O-Pb bond in enzyme-...
The cognate chaperones coordinate with the ClpP in substrate recognition, unfolding the substrate using energy derived from the ATP hydrolysis and delivering the unfolded polypeptide into a proteolytic compartment of the ClpP [53]. The chaperone ClpX self-associates into a hexamer and employs its ...
This trapped ATP molecule proved to be committed to hydrolysis, since it was impossible to exchange it for unbound ATP. This conformational change requires parts of the protein that are C-terminal to the binding site. A conformational change was also observed in the crystal structure of the ...