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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Autor*in
Kumar, Anil;
Manimekalai, Malathy Sony Subramanian;
Balakrishna, Asha Manikkoth;
Hunke, Cornelia;
Weigelt, Sven;
Sewald, NorbertUniBi ;
Grueber, Gerhard
Einrichtung
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.
Stichworte
F1FO ATP synthase;
V-ATPase;
crystal structure;
Methanosarcina mazei Go1;
Methanococcus jannaschii;
archaeal ATPase;
A(1)A(O) ATP synthase
Erscheinungsjahr
2009
Zeitschriftentitel
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Band
75
Ausgabe
4
Seite(n)
807-819
ISSN
0887-3585
eISSN
1097-0134
Page URI
https://pub.uni-bielefeld.de/record/1633800
Zitieren
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. https://doi.org/10.1002/prot.22289
Kumar, Anil, Manimekalai, Malathy Sony Subramanian, Balakrishna, Asha Manikkoth, Hunke, Cornelia, Weigelt, Sven, Sewald, Norbert, and Grueber, Gerhard. 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.
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.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
UNIPROT
1 Eintrag gefunden, die diesen Artikel zitieren
V-type ATP synthase beta chain (UNIPROT: Q60187)
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Download in FASTA format
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Download in FASTA format
PDB
5 Einträge gefunden, die diesen Artikel zitieren
x-ray diffraction (PDB: 3ssa)
Protein structure name: crystal structure of subunit b mutant n157t of the a1ao atp synthase
Public wwPDB file in PDB format
Protein structure name: crystal structure of subunit b mutant n157t of the a1ao atp synthase
Public wwPDB file in PDB format
x-ray diffraction (PDB: 3tgw)
Protein structure name: crystal structure of subunit b mutant h156a of the a1ao atp synthase
Public wwPDB file in PDB format
Protein structure name: crystal structure of subunit b mutant h156a of the a1ao atp synthase
Public wwPDB file in PDB format
x-ray diffraction (PDB: 3tiv)
Protein structure name: crystal structure of subunit b mutant n157a of the a1ao atp synthase
Public wwPDB file in PDB format
Protein structure name: crystal structure of subunit b mutant n157a of the a1ao atp synthase
Public wwPDB file in PDB format
x-ray diffraction (PDB: 3b2q)
Protein structure name: intermediate position of atp on its trail to the binding pocket inside the subunit b mutant r416w of the energy converter a1ao atp synthase
Public wwPDB file in PDB format
Protein structure name: intermediate position of atp on its trail to the binding pocket inside the subunit b mutant r416w of the energy converter a1ao atp synthase
Public wwPDB file in PDB format
x-ray diffraction (PDB: 2rkw)
Protein structure name: intermediate position of atp on its trail to the binding pocket inside the subunit b mutant r416w of the energy converter a1ao atp synthase
Public wwPDB file in PDB format
Protein structure name: intermediate position of atp on its trail to the binding pocket inside the subunit b mutant r416w of the energy converter a1ao atp synthase
Public wwPDB file in PDB format
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PMID: 17082766
Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM., EMBO J. 25(22), 2006
PMID: 17082766
Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy.
Bernal RA, Stock D., Structure 12(10), 2004
PMID: 15458628
Bernal RA, Stock D., Structure 12(10), 2004
PMID: 15458628
NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B.
Gayen S, Vivekanandan S, Biukovic G, Gruber G, Yoon HS., Biochemistry 46(42), 2007
PMID: 17910473
Gayen S, Vivekanandan S, Biukovic G, Gruber G, Yoon HS., Biochemistry 46(42), 2007
PMID: 17910473
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