scholarly journals Location of the genes for cytochrome f, subunit IV of the b6/f complex, the α-subunit of CF1 ATP-synthase and subunit III of the CFα ATP-synthase on the barley chloroplast genome

1984 ◽  
Vol 49 (6) ◽  
pp. 555-557 ◽  
Author(s):  
Richard P. Oliver
Keyword(s):  
Chloroplast Genome ◽  
Atp Synthase ◽  
Cytochrome F ◽  
Α Subunit ◽  
Subunit Iii ◽  
Barley Chloroplast

scholarly journals Targeting Mycobacterial F-ATP Synthase C-Terminal α Subunit Interaction Motif on Rotary Subunit γ

Antibiotics ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1456
Author(s):  
Amaravadhi Harikishore ◽  
Chui-Fann Wong ◽  
Priya Ragunathan ◽  
Dennis Litty ◽  
Volker Müller ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Atp Synthesis ◽  
Membrane Vesicles ◽  
Α Subunit ◽  
Rotational States ◽  
C Terminus ◽  
Inverted Membrane Vesicles ◽  
Hydrolysis Of ◽  
Micromolar Range

Mycobacteria regulate their energy (ATP) levels to sustain their survival even in stringent living conditions. Recent studies have shown that mycobacteria not only slow down their respiratory rate but also block ATP hydrolysis of the F-ATP synthase (α3:β3:γ:δ:ε:a:b:b’:c9) to maintain ATP homeostasis in situations not amenable for growth. The mycobacteria-specific α C-terminus (α533-545) has unraveled to be the major regulative of latent ATP hydrolysis. Its deletion stimulates ATPase activity while reducing ATP synthesis. In one of the six rotational states of F-ATP synthase, α533-545 has been visualized to dock deep into subunit γ, thereby blocking rotation of γ within the engine. The functional role(s) of this C-terminus in the other rotational states are not clarified yet and are being still pursued in structural studies. Based on the interaction pattern of the docked α533-545 region with subunit γ, we attempted to study the druggability of the α533-545 motif. In this direction, our computational work has led to the development of an eight-featured α533-545 peptide pharmacophore, followed by database screening, molecular docking, and pose selection, resulting in eleven hit molecules. ATP synthesis inhibition assays using recombinant ATP synthase as well as mycobacterial inverted membrane vesicles show that one of the hits, AlMF1, inhibited the mycobacterial F-ATP synthase in a micromolar range. The successful targeting of the α533-545-γ interaction motif demonstrates the potential to develop inhibitors targeting the α site to interrupt rotary coupling with ATP synthesis.

scholarly journals Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis

2021 ◽  
Vol 118 (47) ◽  
pp. e2111899118
Author(s):  
Martin G. Montgomery ◽  
Jessica Petri ◽  
Tobias E. Spikes ◽  
John E. Walker
Keyword(s):  
Atp Synthase ◽  
Mycobacterium Smegmatis ◽  
Atp Hydrolysis ◽  
Terminal Region ◽  
Catalytic Cycle ◽  
Α Subunit ◽  
Antitubercular Drugs ◽  
Safe Mechanism ◽  
Fail Safe ◽  
Α Subunits

The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from Mycobacterium smegmatis. This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360° catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an α-subunit in a loop in the γ-subunit, as proposed before, but also a “fail-safe” mechanism involving the b′-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bδ-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the α-subunits. The auto-inhibitory plus the associated “fail-safe” mechanisms and the modes of attachment of the α-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel.

scholarly journals Analysis of Sequence Determinants of F1Fo-ATP Synthase in the N-terminal Region of α Subunit for Binding of δ Subunit

2004 ◽  
Vol 279 (24) ◽  
pp. 25673-25679 ◽  
Author(s):  
Joachim Weber ◽  
Alma Muharemagic ◽  
Susan Wilke-Mounts ◽  
Alan E. Senior
Keyword(s):  
Atp Synthase ◽  
Terminal Region ◽  
Α Subunit ◽  
F1fo Atp Synthase

Male-Biased Mutation Rates Revealed from Z and W Chromosome-Linked ATP Synthase α-Subunit (ATP5A1) Sequences in Birds

2000 ◽  
Vol 50 (5) ◽  
pp. 443-447 ◽  
Author(s):  
Ariane N. Carmichael ◽  
Anna-Karin Fridolfsson ◽  
Joy Halverson ◽  
Hans Ellegren
Keyword(s):  
Atp Synthase ◽  
Mutation Rates ◽  
W Chromosome ◽  
Α Subunit

The Antigenic Structure of the Human Glycoprotein Hormone α-Subunit: III. Solution- and Solid-Phase Mapping Using Synthetic Peptides*

Endocrinology ◽  
1991 ◽  
Vol 128 (6) ◽  
pp. 2907-2915 ◽  
Author(s):  
M. C. CHARLESWORTH ◽  
E. R. BERGERT ◽  
J. C. MORRIS ◽  
D. J. McCORMICK ◽  
R. J. RYAN
Keyword(s):  
Synthetic Peptides ◽  
Solid Phase ◽  
Antigenic Structure ◽  
Glycoprotein Hormone ◽  
Α Subunit ◽  
Phase Mapping ◽  
Subunit Iii
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