The solution structure of the PufX polypeptide from Rhodobacter sphaeroides

Richard B. Tunnicliffe; Emma C. Ratcliffe; C. Neil Hunter; Mike P. Williamson

doi:10.1016/j.febslet.2006.11.065

The solution structure of the PufX polypeptide from Rhodobacter sphaeroides

Richard B. Tunnicliffe, Emma C. Ratcliffe, C. Neil Hunter, Mike P. Williamson

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

Abstract

PufX organises the photosynthetic reaction centre-light harvesting complex 1 (RC-LH1) core complex of Rhodobacter sphaeroides and facilitates quinol/quinone exchange between the RC and cytochrome bc1 complexes. The structure of PufX in organic solvent reveals two hydrophobic helices flanked by unstructured termini and connected by a helical bend. The proposed location of basic residues and tryptophans at the membrane interface orients the C-terminal helix along the membrane normal, with the GXXXG motifs in positions unsuitable as direct drivers of dimerisation of the RC-LH1 complex. The N-terminal helix is predicted to extend ∼40 Å along the membrane interface. © 2006 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	6967-6971
Number of pages	4
Journal	FEBS Letters
Volume	580
Issue number	30
DOIs	https://doi.org/10.1016/j.febslet.2006.11.065
Publication status	Published - 22 Dec 2006

Keywords

Light harvesting
Membrane protein
NMR structure
Photosynthesis
Reaction centre
Rhodobacter sphaeroides

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10.1016/j.febslet.2006.11.065

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title = "The solution structure of the PufX polypeptide from Rhodobacter sphaeroides",

abstract = "PufX organises the photosynthetic reaction centre-light harvesting complex 1 (RC-LH1) core complex of Rhodobacter sphaeroides and facilitates quinol/quinone exchange between the RC and cytochrome bc1 complexes. The structure of PufX in organic solvent reveals two hydrophobic helices flanked by unstructured termini and connected by a helical bend. The proposed location of basic residues and tryptophans at the membrane interface orients the C-terminal helix along the membrane normal, with the GXXXG motifs in positions unsuitable as direct drivers of dimerisation of the RC-LH1 complex. The N-terminal helix is predicted to extend ∼40 {\AA} along the membrane interface. {\textcopyright} 2006 Federation of European Biochemical Societies.",

keywords = "Light harvesting, Membrane protein, NMR structure, Photosynthesis, Reaction centre, Rhodobacter sphaeroides",

author = "Tunnicliffe, \{Richard B.\} and Ratcliffe, \{Emma C.\} and Hunter, \{C. Neil\} and Williamson, \{Mike P.\}",

year = "2006",

month = dec,

day = "22",

doi = "10.1016/j.febslet.2006.11.065",

language = "English",

volume = "580",

pages = "6967--6971",

journal = "FEBS Letters",

publisher = "John Wiley \& Sons Ltd",

number = "30",

}

TY - JOUR

T1 - The solution structure of the PufX polypeptide from Rhodobacter sphaeroides

AU - Tunnicliffe, Richard B.

AU - Ratcliffe, Emma C.

AU - Hunter, C. Neil

AU - Williamson, Mike P.

PY - 2006/12/22

Y1 - 2006/12/22

N2 - PufX organises the photosynthetic reaction centre-light harvesting complex 1 (RC-LH1) core complex of Rhodobacter sphaeroides and facilitates quinol/quinone exchange between the RC and cytochrome bc1 complexes. The structure of PufX in organic solvent reveals two hydrophobic helices flanked by unstructured termini and connected by a helical bend. The proposed location of basic residues and tryptophans at the membrane interface orients the C-terminal helix along the membrane normal, with the GXXXG motifs in positions unsuitable as direct drivers of dimerisation of the RC-LH1 complex. The N-terminal helix is predicted to extend ∼40 Å along the membrane interface. © 2006 Federation of European Biochemical Societies.

AB - PufX organises the photosynthetic reaction centre-light harvesting complex 1 (RC-LH1) core complex of Rhodobacter sphaeroides and facilitates quinol/quinone exchange between the RC and cytochrome bc1 complexes. The structure of PufX in organic solvent reveals two hydrophobic helices flanked by unstructured termini and connected by a helical bend. The proposed location of basic residues and tryptophans at the membrane interface orients the C-terminal helix along the membrane normal, with the GXXXG motifs in positions unsuitable as direct drivers of dimerisation of the RC-LH1 complex. The N-terminal helix is predicted to extend ∼40 Å along the membrane interface. © 2006 Federation of European Biochemical Societies.

KW - Light harvesting

KW - Membrane protein

KW - NMR structure

KW - Photosynthesis

KW - Reaction centre

KW - Rhodobacter sphaeroides

U2 - 10.1016/j.febslet.2006.11.065

DO - 10.1016/j.febslet.2006.11.065

M3 - Article

VL - 580

SP - 6967

EP - 6971

JO - FEBS Letters

JF - FEBS Letters

IS - 30

ER -

The solution structure of the PufX polypeptide from Rhodobacter sphaeroides

Abstract

Keywords

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