NDLI: Role of α-Subunit VISIT-DG Sequence Residues Ser-347 and Gly-351 in the Catalytic Sites of Escherichia coli ATP Synthase*

Content Provider	PubMed Central
Author	Li, Wenzong Brudecki, Laura E. Senior, Alan E. Ahmad, Zulfiqar
Abstract	This paper describes the role of α-subunit VISIT-DG sequence residues αSer-347 and αGly-351 in catalytic sites of Escherichia coli F1Fo ATP synthase. X-ray structures show the very highly conserved α-subunit VISIT-DG sequence in close proximity to the conserved phosphate-binding residues αArg-376, βArg-182, βLys-155, and βArg-246 in the phosphate-binding subdomain. Mutations αS347Q and αG351Q caused loss of oxidative phosphorylation and reduced ATPase activity of F1Fo in membranes by 100- and 150-fold, respectively, whereas αS347A mutation showed only a 13-fold loss of activity and also retained some oxidative phosphorylation activity. The ATPase of αS347Q mutant was not inhibited, and the αS347A mutant was slightly inhibited by MgADP-azide, MgADP-fluoroaluminate, or MgADP-fluoroscandium, in contrast to wild type and αG351Q mutant. Whereas 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole (NBD-Cl) inhibited wild type and αG351Q mutant ATPase essentially completely, ATPase in αS347A or αS347Q mutant was inhibited maximally by ∼80–90%, although reaction still occurred at residue βTyr-297, proximal to the α-subunit VISIT-DG sequence, near the phosphate-binding pocket. Inhibition characteristics supported the conclusion that NBD-Cl reacts inβE (empty) catalytic sites, as shown previously by x-ray structure analysis. Phosphate protected against NBD-Cl inhibition in wild type and αG351Q mutant but not in αS347Q or αS347A mutant. The results demonstrate that αSer-347 is an additional residue involved in phosphate-binding and transition state stabilization in ATP synthase catalytic sites. In contrast, αGly-351, although strongly conserved and clearly important for function, appears not to play a direct role.
Related Links	http://dx.doi.org/10.1074/jbc.m809209200
Ending Page	10754
Page Count	8
Starting Page	10747
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	16
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2009-02-01
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Role of α-Subunit VISIT-DG Sequence Residues Ser-347 and Gly-351 in the Catalytic Sites of Escherichia coli ATP Synthase

Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.

Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase

Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site.

Mechanism of Inhibition by C-terminal α-Helices of the ϵ Subunit of Escherichia coli FoF1-ATP Synthase*

Role of the conserved Lys-X-Gly-Gly sequence at the ADP-glucose-binding site in Escherichia coli glycogen synthase.

Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm*

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Role of α-Subunit VISIT-DG Sequence Residues Ser-347 and Gly-351 in the Catalytic Sites of Escherichia coli ATP Synthase*

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