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Showing 1 to 3 of 3 for “"VISIT-DG"”.
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Role of a-Subunit VISIT-DG Sequence Residues Ile-346 and Ile-348 in the Catalytic Sites of Escherichia Coli ATP Synthase.
… One of them is the highly conserved α-subunit VISIT-DG sequence that is close to the Pi binding subdomain. The questions arise "Are they involved in Pi binding? Or are they there simply for the structural integrity of the catalytic sites?" Here, αIle-346and αIle-348, two important residues of …
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Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of <em>Escherichia coli</em> ATP Synthase.
… in Pi binding have to be identified. The αVISIT-DG sequence at the interface of α/β subunits that contains residues from 345-351 is highly conserved and αAsp-350 has been chosen because of its negative charge side chain and its close proximity (~2.8 Å) to the known phosphate binding residue …
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Modulation of Alpha-Subunit VISIT-DG Sequence Residues Ser-347, Gly-351 and Thr-349 in the Catalytic Sites of <em>Escherichia coli</em> ATP Synthase.
… the role of highly conserved α-subunit VISIT-DG sequence residues αSer-347, αGly-351, and αThr-349 in P<sub>i</sub> binding. Mutations αS347A/Q, αG351Q, αT349A/D/R, βR182A, and αT349R/βR182A were generated via site directed mutagenesis. Results from biochemical assays showed that …