Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.

doi:10.1021/bi5013063

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Article

Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.

Biochemistry - 2 Dec 2014

Ahmad Zulfiqar, Winjobi Mumeenat, Kabir M Anaul

Abstract excerpt

This paper describes the role of α-subunit VISIT-DG sequence residue αThr-349 in the catalytic sites of Escherichia coli F1Fo ATP synthase. X-ray structures show the highly conserved αThr-349 in the proximity (2.68 Å) of the conserved phosphate binding residue βR182 in the phosphate binding subdomain. αT349A, -D, -Q, and -R mutations caused 90-100-fold losses of oxidative phosphorylation and reduced ATPase...

Topics

Adenosine Diphosphate
Aluminum
Azides
Catalytic Domain
Cell Membrane
Dicyclohexylcarbodiimide
Dithiothreitol
Enzyme Inhibitors
Escherichia coli
Fluorine
Mitochondrial Proton-Translocating ATPases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Mutagenesis

Mutation

Nitrobenzenes

Oxazoles

Threonine

Source

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Identifiers

PMID: 25375895
DOI: 10.1021/bi5013063
PMCID: PMC4255642

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