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The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.

Manimekalai MS, Kumar A, Jeyakanthan J, Grüber G
J Mol Biol 408 736-54 (2011)
Related entries: 3i4l, 3i72, 3i73, 3ikj, 3nd9, 3p20

Cited: 4 times
EuropePMC logo PMID: 21396943

Abstract

Archaeal A-ATP synthases catalyze the formation of the energy currency ATP. The chemical mechanisms of ATP synthesis in A-ATP synthases are unknown. We have determined the crystal structure of a transition-like state of the vanadate-bound form of catalytic subunit A (A(Vi)) of the A-ATP synthase from Pyrococcus horikoshii OT3. Two orthovanadate molecules were observed in the A(Vi) structure, one of which interacts with the phosphate binding loop through residue S238. The second vanadate is positioned in the transient binding site, implicating for the first time the pathway for phosphate entry to the catalytic site. Moreover, since residues K240 and T241 are proposed to be essential for catalysis, the mutant structures of K240A and T241A were also determined. The results demonstrate the importance of these two residues for transition-state stabilization. The structures presented shed light on the diversity of catalytic mechanisms used by the biological motors A- and F-ATP synthases and eukaryotic V-ATPases.

Reviews citing this publication (1)

  1. ATP synthases from archaea: the beauty of a molecular motor. Grüber G, Manimekalai MS, Mayer F, Müller V. Biochim Biophys Acta 1837 940-952 (2014)

Articles citing this publication (3)

  1. Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans. Mohanty S, Jobichen C, Chichili VPR, Velázquez-Campoy A, Low BC, Hogue CWV, Sivaraman J. J Biol Chem 290 27280-27296 (2015)
  2. Relevance of the conserved histidine and asparagine residues in the phosphate-binding loop of the nucleotide binding subunit B of A₁A₀ ATP synthases. Tadwal VS, Sundararaman L, Manimekalai MS, Hunke C, Grüber G. J Struct Biol 180 509-518 (2012)
  3. Conserved glycine residues in the P-loop of ATP synthases form a doorframe for nucleotide entrance. Priya R, Kumar A, Manimekalai MS, Grüber G. J Mol Biol 413 657-666 (2011)


Related citations provided by authors (2)

  1. 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 396 301-20 (2010)
  2. Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk.. Maegawa Y, Morita H, Iyaguchi D, Yao M, Watanabe N, Tanaka I Acta Crystallogr D Biol Crystallogr 62 483-8 (2006)

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