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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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| Huvudupphovsmän: | , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
International Union of Crystallography
2011
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| Ämnen: | |
| Länkar: | 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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