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

<p>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.</p>

Name thesis:degree_name

MS (Master of Science)

Level thesis:degree_level

Thesis - unrestricted

Discipline thesis:degree_discipline

Biology

Year dc:date.issued

2011

Author dc:creator

• Jonnalagadda, Sneha R

• F1Fo- ATP Synthase
• ATP Synthesis
• E coli
• biological nanomotor
• VISIT-DG Sequence
• NBD-Cl
• Aluminum chloride
• Scandium chloride
• DCCD
• DTT
• Mg-ADP.
• Biochemistry, Biophysics, and Structural Biology
• Life Sciences
• Molecular Biology

Statement dc:rights

• Copyright by the authors.

Repository record dc:identifier

https://dc.etsu.edu/etd/1296

OAI identifier oai:identifier

oai:dc.etsu.edu:etd-2487