Global ETD Search

1	Role of a-Subunit VISIT-DG Sequence Residues Ile-346 and Ile-348 in the Catalytic Sites of Escherichia Coli ATP Synthase. Zhao, Chao 07 May 2011 (has links) (PDF) F1FO-ATP synthase is the primary source of cellular energy production in most living organisms. Malfunction of this enzyme is implicated in diseases. There are many functional motifs in and around the catalytic sites of this enzyme. 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 the conserved VISIT-DG sequence, are discussed. Each residue was mutated to A/R/D/Q. Growth assays in limiting glucose media and on succinate plates suggests αIle-346 and αIle-348 are critical for the normal enzymatic function (oxidative phosphorylation). And the biochemical assays do suggest both αI-346 and αI-348 are required to maintain catalytic site, involved in Pi binding indirectly, but αI-348 plays more important role than αI-346. ATP synthase VISIT-DG sequence Pi binding Life Sciences Molecular Biology
2	Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of <em>Escherichia coli</em> ATP Synthase. Jonnalagadda, Sneha R 01 May 2011 (has links) ATP Synthase is the fundamental means of cellular energy production in animals, plants, and almost all microorganisms. In order to understand the mechanism of ATP catalysis, critical amino acid residues involved 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 αArg-376. The mutant's αD350R, αD350Q, αD350A, αR376A/D, and αG351R/A/D were generated by site directed mutagenesis and several biochemical assays were performed on them to understand the role played by the amino acid residues in Pi binding. Biochemical results suggest that αD350 may be involved in catalysis of ATP synthase and play an important role in Pi binding, whereas αG351 may be involved only in the structural integrity. F1Fo- ATP Synthase ATP Synthesis E coli biological nanomotor VISIT-DG Sequence NBD-Cl Aluminum chloride Scandium chloride DCCD DTT Mg-ADP. Life Sciences Molecular Biology

Search results

Role of a-Subunit VISIT-DG Sequence Residues Ile-346 and Ile-348 in the Catalytic Sites of Escherichia Coli ATP Synthase.

Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of <em>Escherichia coli</em> ATP Synthase.