Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase

Kumar A, Manimekalai MSS, Balakrishna AM, Hunke C, Weigelt S, Sewald N, Grueber G (2009)
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 75(4): 807-819.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
A strategically placed tryptophan in position of Arg416 was used as an optical probe to monitor adenosine triphosphate and adenosine-diphosphate binding to subunit B of the A(1)A(O) adenosine triphosphate (ATP) synthase from Methanosarcina mazei Go1. Tryptophan fluorescence and fluorescence correlation spectroscopy gave binding constants indicating a preferred binding of ATP over ADP to the protein. The X-ray crystal structure of the R416W mutant protein in the presence of ATP was solved to 2.1 angstrom resolution, showing the substituted Trp-residue inside the predicted adenine-binding pocket. The cocrystallized ATP molecule could be trapped in a so-called transition nucleotide-binding state. The high resolution structure shows the phosphate residues of the ATP near the P-loop region (S150-E158) and its adenine ring forms pi-pi interaction with Phe149. This transition binding position of ATP could be confirmed by tryptophan emission spectra using the subunit B mutant F149W. The trapped ATP position, similar to the one of the binding region of the antibiotic efrapeptin in F1FO ATP synthases, is discussed in light of a transition nucleotide-binding state of ATP while on its way to the final binding pocket. Finally, the inhibitory effect of efrapeptin C in ATPase activity of a reconstituted A(3)B(3)- and A(3)B(R416W)(3)-subcomplex, composed of subunit A and the B subunit mutant R416W, of the A(1)A(O) ATP synthase is shown.
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Zeitschriftentitel
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Band
75
Zeitschriftennummer
4
Seite
807-819
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eISSN
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Kumar A, Manimekalai MSS, Balakrishna AM, et al. Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS. 2009;75(4):807-819.
Kumar, A., Manimekalai, M. S. S., Balakrishna, A. M., Hunke, C., Weigelt, S., Sewald, N., & Grueber, G. (2009). Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 75(4), 807-819. doi:10.1002/prot.22289
Kumar, A., Manimekalai, M. S. S., Balakrishna, A. M., Hunke, C., Weigelt, S., Sewald, N., and Grueber, G. (2009). Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 75, 807-819.
Kumar, A., et al., 2009. Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 75(4), p 807-819.
A. Kumar, et al., “Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase”, PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, vol. 75, 2009, pp. 807-819.
Kumar, A., Manimekalai, M.S.S., Balakrishna, A.M., Hunke, C., Weigelt, S., Sewald, N., Grueber, G.: Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS. 75, 807-819 (2009).
Kumar, Anil, Manimekalai, Malathy Sony Subramanian, Balakrishna, Asha Manikkoth, Hunke, Cornelia, Weigelt, Sven, Sewald, Norbert, and Grueber, Gerhard. “Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A(1)A(O) ATP synthase”. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 75.4 (2009): 807-819.

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Conformational properties of secondary amino acids: replacement of pipecolic acid by N-methyl-l-alanine in efrapeptin C.
Dutt Konar A, Vass E, Hollósi M, Majer Z, Grüber G, Frese K, Sewald N., Chem Biodivers 10(5), 2013
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Synthesis and conformational analysis of efrapeptins.
Weigelt S, Huber T, Hofmann F, Jost M, Ritzefeld M, Luy B, Freudenberger C, Majer Z, Vass E, Greie JC, Panella L, Kaptein B, Broxterman QB, Kessler H, Altendorf K, Hollósi M, Sewald N., Chemistry 18(2), 2012
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Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A(1)A(O) ATP synthase of Methanosarcina mazei Gö1.
Raghunathan D, Gayen S, Kumar A, Hunke C, Grüber G, Verma CS., J Bioenerg Biomembr 44(1), 2012
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The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
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Nucleotide binding states of subunit A of the A-ATP synthase and the implication of P-loop switch in evolution.
Kumar A, Manimekalai MS, Balakrishna AM, Jeyakanthan J, Grüber G., J Mol Biol 396(2), 2010
PMID: 19944110
Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering.
Balakrishna AM, Manimekalai MS, Hunke C, Gayen S, Rössle M, Jeyakanthan J, Grüber G., J Bioenerg Biomembr 42(4), 2010
PMID: 20571891
The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding.
Kumar A, Manimekalai MS, Balakrishna AM, Priya R, Biuković G, Jeyakanthan J, Grüber G., J Mol Biol 401(5), 2010
PMID: 20615420

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