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PDBsum entry 2hg9
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Photosynthesis/membrane protein
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PDB id
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2hg9
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Contents |
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281 a.a.
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302 a.a.
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241 a.a.
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* Residue conservation analysis
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PDB id:
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Photosynthesis/membrane protein
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Title:
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Reaction centre from rhodobacter sphaeroides strain r-26.1 complexed with tetrabrominated phosphatidylcholine
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Structure:
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Reaction center protein l chain. Chain: l. Synonym: photosynthetic reaction center l subunit. Reaction center protein m chain. Chain: m. Synonym: photosynthetic reaction center m subunit. Reaction center protein h chain. Chain: h. Synonym: photosynthetic reaction center h subunit
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Source:
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Rhodobacter sphaeroides. Organism_taxid: 1063. Strain: r26.1. Other_details: strain r-26.1 of rhodobacter sphaeroides bacteria is a partial revertant of the r-26 chemical mutant of the wild-type strain 2.4.1. While r-26 has no lh2 antenna and no carotenoid, the r-26.1 has altered lh2 antenna and no carotenoid. Reaction center from r-26.1 strain is therefore identical with the wild-type strain 2.4.1 except for the missing carotenoid..
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Resolution:
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2.45Å
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R-factor:
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0.180
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R-free:
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0.209
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Authors:
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A.W.Roszak,A.T.Gardiner,N.W.Isaacs,R.J.Cogdell
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Key ref:
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A.W.Roszak
et al.
(2007).
Brominated lipids identify lipid binding sites on the surface of the reaction center from Rhodobacter sphaeroides.
Biochemistry,
46,
2909-2916.
PubMed id:
DOI:
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Date:
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26-Jun-06
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Release date:
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27-Mar-07
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PROCHECK
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Headers
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References
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P0C0Y8
(RCEL_CERSP) -
Reaction center protein L chain from Cereibacter sphaeroides
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Seq: Struc:
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282 a.a.
281 a.a.
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Enzyme class:
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Chains L, M, H:
E.C.?
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DOI no:
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Biochemistry
46:2909-2916
(2007)
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PubMed id:
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Brominated lipids identify lipid binding sites on the surface of the reaction center from Rhodobacter sphaeroides.
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A.W.Roszak,
A.T.Gardiner,
N.W.Isaacs,
R.J.Cogdell.
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ABSTRACT
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This study describes the use of brominated phospholipids to distinguish between
lipid and detergent binding sites on the surface of a typical alpha-helical
membrane protein. Reaction centers isolated from Rhodobacter sphaeroides were
cocrystallized with added brominated phospholipids. X-ray structural analysis of
these crystals has revealed the presence of two lipid binding sites from the
characteristic strong X-ray scattering from the bromine atoms. These results
demonstrate the usefulness of this approach to mapping lipid binding sites at
the surface of membrane proteins.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.Arias-Cartin,
S.Grimaldi,
J.Pommier,
P.Lanciano,
C.Schaefer,
P.Arnoux,
G.Giordano,
B.Guigliarelli,
and
A.Magalon
(2011).
Cardiolipin-based respiratory complex activation in bacteria.
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Proc Natl Acad Sci U S A,
108,
7781-7786.
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R.M.Bill,
P.J.Henderson,
S.Iwata,
E.R.Kunji,
H.Michel,
R.Neutze,
S.Newstead,
B.Poolman,
C.G.Tate,
and
H.Vogel
(2011).
Overcoming barriers to membrane protein structure determination.
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Nat Biotechnol,
29,
335-340.
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C.A.Kors,
E.Wallace,
D.R.Davies,
L.Li,
P.D.Laible,
and
P.Nollert
(2009).
Effects of impurities on membrane-protein crystallization in different systems.
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Acta Crystallogr D Biol Crystallogr,
65,
1062-1073.
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L.Qin,
M.A.Sharpe,
R.M.Garavito,
and
S.Ferguson-Miller
(2007).
Conserved lipid-binding sites in membrane proteins: a focus on cytochrome c oxidase.
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Curr Opin Struct Biol,
17,
444-450.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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');
}
}
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