Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly

Ragunathan Priya; Vikeramjeet S Tadwal; Manfred W Roessle; Shovanlal Gayen; Cornelia Hunke; Weng Chuan Peng; Jaume Torres; Gerhard Grüber

doi:10.1007/s10863-008-9154-x

Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly

Ragunathan Priya, Vikeramjeet S Tadwal, Manfred W Roessle, Shovanlal Gayen, Cornelia Hunke, Weng Chuan Peng, Jaume Torres, Gerhard Grüber

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

The first low resolution solution structure of the soluble domain of subunit b (b (22-156)) of the Escherichia coli F(1)F(O) ATPsynthase was determined from small-angle X-ray scattering data. The dimeric protein has a boomerang-like shape with a total length of 16.2 +/- 0.3 nm. Fluorescence correlation spectroscopy (FCS) shows that the protein binds effectively to the subunit delta, confirming their described neighborhood. Using the recombinant C-terminal domain (delta(91-177)) of subunit delta and the C-terminal peptides of subunit b, b (120-140) and b (140-156), FCS titration experiments were performed to assign the segments involved in delta-b assembly. These data identify the very C-terminal tail b (140-156) to interact with delta(91-177). The novel 3D structure of this peptide has been determined by NMR spectroscopy. The molecule adopts a stable helix formation in solution with a flexible tail between amino acid 140 to 145.

Original language	English
Pages (from-to)	245-55
Number of pages	11
Journal	Journal of bioenergetics and biomembranes
Volume	40
Issue number	4
DOIs	https://doi.org/10.1007/s10863-008-9154-x
Publication status	Published - Aug 2008
Externally published	Yes

Keywords

Adenosine Triphosphate/chemistry
Bacterial Proton-Translocating ATPases/chemistry
Binding Sites
Computer Simulation
Enzyme Activation
Enzyme Stability
Escherichia coli/enzymology
Magnetic Resonance Spectroscopy
Models, Chemical
Models, Molecular
Protein Binding
Protein Conformation
Protein Subunits/chemistry

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10.1007/s10863-008-9154-x

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title = "Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly",

abstract = "The first low resolution solution structure of the soluble domain of subunit b (b (22-156)) of the Escherichia coli F(1)F(O) ATPsynthase was determined from small-angle X-ray scattering data. The dimeric protein has a boomerang-like shape with a total length of 16.2 +/- 0.3 nm. Fluorescence correlation spectroscopy (FCS) shows that the protein binds effectively to the subunit delta, confirming their described neighborhood. Using the recombinant C-terminal domain (delta(91-177)) of subunit delta and the C-terminal peptides of subunit b, b (120-140) and b (140-156), FCS titration experiments were performed to assign the segments involved in delta-b assembly. These data identify the very C-terminal tail b (140-156) to interact with delta(91-177). The novel 3D structure of this peptide has been determined by NMR spectroscopy. The molecule adopts a stable helix formation in solution with a flexible tail between amino acid 140 to 145.",

keywords = "Adenosine Triphosphate/chemistry, Bacterial Proton-Translocating ATPases/chemistry, Binding Sites, Computer Simulation, Enzyme Activation, Enzyme Stability, Escherichia coli/enzymology, Magnetic Resonance Spectroscopy, Models, Chemical, Models, Molecular, Protein Binding, Protein Conformation, Protein Subunits/chemistry",

author = "Ragunathan Priya and Tadwal, {Vikeramjeet S} and Roessle, {Manfred W} and Shovanlal Gayen and Cornelia Hunke and Peng, {Weng Chuan} and Jaume Torres and Gerhard Gr{\"u}ber",

note = "Funding Information: Acknowledgment This research and the fellowships for R. Priya as well as for V. S. Tadwal were supported by a grant from the Ministry of Education, Singapore (ARC 6/06 and RG144/06). S. Gayen is a recipient of the Graduate Research Scholarship, Nanyang Technological University, Singapore.",

year = "2008",

month = aug,

doi = "10.1007/s10863-008-9154-x",

language = "English",

volume = "40",

pages = "245--55",

journal = "Journal of bioenergetics and biomembranes",

issn = "0145-479X",

publisher = "Springer",

number = "4",

}

TY - JOUR

T1 - Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly

AU - Priya, Ragunathan

AU - Tadwal, Vikeramjeet S

AU - Roessle, Manfred W

AU - Gayen, Shovanlal

AU - Hunke, Cornelia

AU - Peng, Weng Chuan

AU - Torres, Jaume

AU - Grüber, Gerhard

N1 - Funding Information: Acknowledgment This research and the fellowships for R. Priya as well as for V. S. Tadwal were supported by a grant from the Ministry of Education, Singapore (ARC 6/06 and RG144/06). S. Gayen is a recipient of the Graduate Research Scholarship, Nanyang Technological University, Singapore.

PY - 2008/8

Y1 - 2008/8

N2 - The first low resolution solution structure of the soluble domain of subunit b (b (22-156)) of the Escherichia coli F(1)F(O) ATPsynthase was determined from small-angle X-ray scattering data. The dimeric protein has a boomerang-like shape with a total length of 16.2 +/- 0.3 nm. Fluorescence correlation spectroscopy (FCS) shows that the protein binds effectively to the subunit delta, confirming their described neighborhood. Using the recombinant C-terminal domain (delta(91-177)) of subunit delta and the C-terminal peptides of subunit b, b (120-140) and b (140-156), FCS titration experiments were performed to assign the segments involved in delta-b assembly. These data identify the very C-terminal tail b (140-156) to interact with delta(91-177). The novel 3D structure of this peptide has been determined by NMR spectroscopy. The molecule adopts a stable helix formation in solution with a flexible tail between amino acid 140 to 145.

AB - The first low resolution solution structure of the soluble domain of subunit b (b (22-156)) of the Escherichia coli F(1)F(O) ATPsynthase was determined from small-angle X-ray scattering data. The dimeric protein has a boomerang-like shape with a total length of 16.2 +/- 0.3 nm. Fluorescence correlation spectroscopy (FCS) shows that the protein binds effectively to the subunit delta, confirming their described neighborhood. Using the recombinant C-terminal domain (delta(91-177)) of subunit delta and the C-terminal peptides of subunit b, b (120-140) and b (140-156), FCS titration experiments were performed to assign the segments involved in delta-b assembly. These data identify the very C-terminal tail b (140-156) to interact with delta(91-177). The novel 3D structure of this peptide has been determined by NMR spectroscopy. The molecule adopts a stable helix formation in solution with a flexible tail between amino acid 140 to 145.

KW - Adenosine Triphosphate/chemistry

KW - Bacterial Proton-Translocating ATPases/chemistry

KW - Binding Sites

KW - Computer Simulation

KW - Enzyme Activation

KW - Enzyme Stability

KW - Escherichia coli/enzymology

KW - Magnetic Resonance Spectroscopy

KW - Models, Chemical

KW - Models, Molecular

KW - Protein Binding

KW - Protein Conformation

KW - Protein Subunits/chemistry

UR - http://www.scopus.com/inward/record.url?scp=56349125095&partnerID=8YFLogxK

U2 - 10.1007/s10863-008-9154-x

DO - 10.1007/s10863-008-9154-x

M3 - Article

C2 - 18668355

SN - 0145-479X

VL - 40

SP - 245

EP - 255

JO - Journal of bioenergetics and biomembranes

JF - Journal of bioenergetics and biomembranes

IS - 4

ER -

Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly

Abstract

Keywords

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