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The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase
The three-dimensional structure of a soluble variant of TrwB, an integral membrane DNA-binding protein in the Escherichia coli R388 conjugative system, is reported, which consists of a nucleotide-binding domain of α/β topology, reminiscent of RecA and DNA ring helicases, and an all-α domain.
Ectopic β-chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis
The effect of high-density lipoprotein (HDL) in protecting against atherosclerosis is usually attributed to its role in ‘reverse cholesterol transport’. In this process, HDL particles mediate the
Modulation of the Oligomerization State of the Bovine F1-ATPase Inhibitor Protein, IF1, by pH*
The mutation of histidine 49 to lysine is predicted to abolish coiled-coil formation over residues 32–43 preventing interaction between two dimers, forcing the equilibrium toward the dimeric state, thereby freeing the N-terminal inhibitory regions and allowing them to interact with F1.
Characterization of ATP and DNA Binding Activities of TrwB, the Coupling Protein Essential in Plasmid R388 Conjugation*
DNA binding enhanced TrwC nic cleavage, providing the first evidence that directly links TrwB with conjugative DNA processing, and suggest potential functions for conjugatives coupling proteins, both as triggers of conjugATIVE DNA processing and as motors in the transport process.
TrwD, a Protein Encoded by the IncW Plasmid R388, Displays an ATP Hydrolase Activity Essential for Bacterial Conjugation*
The deduced amino acid sequence of TrwD showed homology to the PulE/VirB11 superfamily of potential ATPases involved in various types of transport processes and suggested that GST-TrwD was still able to interact either with itself or with other component(s) of the conjugative machinery.
The structure of bovine F1-ATPase in complex with its regulatory protein IF1
In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1, which implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.
Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation
It is suggested that the factors that determine the frequencies of transfer of different MOB regions are the differential interactions of TrwB with pilus and relaxosome.
Towards an integrated model of bacterial conjugation.
A model for pilus biogenesis and substrate transfer in conjugative systems is proposed and provides a renewed view of the mechanism that might help to envisage new strategies to curb the threating expansion of antibiotic resistance.
TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase.
A mechanism for TrwB as a DNA-translocating motor, sensitive to pH and salt concentration, is proposed, and its structural similarity to F1-ATPase is proposed.
Dimerization of Bovine F1-ATPase by Binding the Inhibitor Protein, IF1 *
In mitochondria, the hydrolytic activity of ATP synthase is regulated by a natural inhibitor protein, IF1, and it is not known whether IF1 can bring about the dimerization of the F1F0-ATPase complex.