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Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy

A reporter tryptophan residue was individually introduced by site-directed mutagenesis into the adenine-binding pocket of the catalytic subunit A (F427W and F508W mutants) of the motor protein A(1)A(O) ATP synthase from Pyrococcus horikoshii OT3. The crystal structures of the F427W and F508W mutant...

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Bibliografiset tiedot
Päätekijät: Tadwal, Vikeramjeet Singh, Manimekalai, Malathy Sony Subramanian, Grüber, Gerhard
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: International Union of Crystallography 2011
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC3232122/
https://ncbi.nlm.nih.gov/pubmed/22139149
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309111039595
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