The Transition-Like State and Pi Entrance into the Catalytic A Subunit of the Biological Engine A-ATP Synthase

Manimekalai, Malathy Sony Subramanian; Kumar, Anil; Jeyakanthan, Jeyaraman; Grüber, Gerhard

doi:10.1016/j.jmb.2011.03.010

Cited by 11 publications

(13 citation statements)

References 39 publications

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“…The vanadate moiety is located next to the P-loop ( 156 GGAGVGKT 163 ) and several residues, not only from the P-loop, are involved in its stabilization, namely Glu188 that acts as the catalytic base [385]. Interestingly, compared to the previously obtained F 1 ATP synthase in the ground state with phosphate (PDB: 1MAB) The other structure was deposited in 2011: a 2.85 Å XRD resolution structure of the catalytic A subunit of A 1 A o ATP synthase from Pyrococcus horikoshii (PDB: 3P20) [389]. This protein, an example from Archaea.…”

Section: Transportersmentioning

confidence: 99%

“…The modeled structure contains two vanadate(V) moieties, placed next to the P-loop (7.94 Å apart from each other), hydrogen bonded to Ser238 and Leu417 residues (1 st and 2 nd vanadate(V), respectively) and also depicting weak non-polar interactions with several other protein residues (but not with water molecules). The significance of the second vanadate(V) (found in the transient binding site) and the importance of the Lys240 and Thr241 residues was discussed using a combined approach which includes mutagenesis, ITC and X-ray Crystallography techniques [389].…”

Section: Transportersmentioning

confidence: 99%

See 1 more Smart Citation

Vanadium and proteins: Uptake, transport, structure, activity and function

Pessoa

Garribba

Santos

et al. 2015

Coordination Chemistry Reviews

183

104

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Section: Transportersmentioning

confidence: 99%

Section: Transportersmentioning

confidence: 99%

Vanadium and proteins: Uptake, transport, structure, activity and function

Pessoa

Garribba

Santos

et al. 2015

Coordination Chemistry Reviews

183

104

View full text Add to dashboard Cite

“…Additionally, in the case of the half-closed state (1h8e_AE), we observed that the sulfur atom of sulfate (P i analogue) was in a nearly identical position relative to the β-carbon of βA158 as found in the transition state-like structure. This might suggest that P-loop geometry is established early, by first binding P i followed by MgADP as supported by the work of Ko et al 35 and Watanabe et al 61 in F-type ATP synthase, and Manimekalai et al 62 in A-type ATP synthase.…”

Section: Alignment Of Catalytic αβ Pairs With a Common Coordinate Sysmentioning

confidence: 76%

Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg²⁺ and P-Loop Residues in Making ATP

Blum

Ko²,

Pedersen

2012

Biochemistry

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The mitochondrial ATP synthase (F(o)F(1)) is one of the most abundant, important, and complex enzymes found in animals and humans. In earlier studies, we used the photosensitive phosphate analogue vanadate (V(i)) to study the enzyme's mechanism in the transition state. Significantly, these studies showed that Mg(2+) plays an important role in transition state formation during ATP synthesis. Additionally, in both MgADP·V(i)-F(1) and MgV(i)-F(1) complexes, photoactivation of orthovanadate (V(i)) induced cleavage at the third residue within the P-loop (GGAGVGKT), i.e., βA158, suggesting its proximity to the γ-phosphate during transition state formation. However, despite our recent release of the F(1)-ATPase structure containing V(i), the structural details regarding the role of Mg(2+) have remained elusive. Therefore, in this study, we sought to improve our understanding of the essential role of Mg(2+) during transition state formation. We utilized Protein Data Bank structural data representing different conformational intermediates of key steps in ATP synthesis to assemble a database of positional relationships between landmark residues of the catalytic site and the bound ligand. Applying novel bioinformatics methods, we combined the resulting interatomic spatial data with an animated model of the catalytic site to visualize the exact nature of the changes in these positional relationships during ATP synthesis. The results of these studies reported here show that the absence of Mg(2+) results in migration of inorganic phosphate (P(i)) from βA158 to a more medial position in the P-loop binding pocket, thereby disrupting essential placement and orientation of the P(i) needed to form the transition state structure and therefore MgATP.

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“…ATP synthases are the most well studied. However, this information is limited to low resolution cryo-EM data and structures of indi- vidual subunits (19,52,57,62,63). To date, there is no crystal structure available for the core complex (A 3 B 3 ) of ATP synthases from archaeal species.…”

Section: Discussionmentioning

confidence: 99%

Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans

Mohanty

Jobichen

Chichili

et al. 2015

Journal of Biological Chemistry

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Background: Structural asymmetry upon nucleotide binding is crucial for catalytic activity of ATP synthases. Results: The structures of apo and bound A 3 B 3 hexamer of N. equitans ATP synthase show conformational inflexibility. Conclusion: The N. equitans A 3 B 3 hexamer is an inactive form. Significance: The structure of inactive form of N. equitans ATP synthase A 3 B 3 is shown for the first time.

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The Transition-Like State and Pi Entrance into the Catalytic A Subunit of the Biological Engine A-ATP Synthase

Cited by 11 publications

References 39 publications

Vanadium and proteins: Uptake, transport, structure, activity and function

Vanadium and proteins: Uptake, transport, structure, activity and function

Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg²⁺ and P-Loop Residues in Making ATP

Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans

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The Transition-Like State and Pi Entrance into the Catalytic A Subunit of the Biological Engine A-ATP Synthase

Cited by 11 publications

References 39 publications

Vanadium and proteins: Uptake, transport, structure, activity and function

Vanadium and proteins: Uptake, transport, structure, activity and function

Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg2+ and P-Loop Residues in Making ATP

Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans

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Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg²⁺ and P-Loop Residues in Making ATP