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* Residue conservation analysis
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DOI no:
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J Struct Biol
126:86-97
(1999)
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PubMed id:
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Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution.
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S.Ritter,
R.G.Hiller,
P.M.Wrench,
W.Welte,
K.Diederichs.
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ABSTRACT
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The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis
was solved at 1.90-A resolution by molecular replacement, using the atomic
coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model.
The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for
reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer
with an internal noncrystallographic dyad and a fragment of the
gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two
covalently bound phycoerythrobilins at positions alpha82 and alpha139. The
beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues
beta82 and beta158 and one phycourobilin covalently attached to rings A and D at
residues beta50 and beta61, respectively. The electron density of the
gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry,
but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two
tyrosine residues of the gamma-polypeptide are in close proximity to the
phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides
and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer.
Possible energy transfer pathways are discussed briefly.
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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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H.N.Su,
B.B.Xie,
X.Y.Zhang,
B.C.Zhou,
and
Y.Z.Zhang
(2010).
The supramolecular architecture, function, and regulation of thylakoid membranes in red algae: an overview.
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Photosynth Res,
106,
73-87.
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M.Kamio,
L.Nguyen,
S.Yaldiz,
and
C.D.Derby
(2010).
How to produce a chemical defense: structural elucidation and anatomical distribution of aplysioviolin and phycoerythrobilin in the sea hare Aplysia californica.
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Chem Biodivers,
7,
1183-1197.
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H.Scheer,
and
K.H.Zhao
(2008).
Biliprotein maturation: the chromophore attachment.
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Mol Microbiol,
68,
263-276.
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M.Dines,
E.Sendersky,
L.David,
R.Schwarz,
and
N.Adir
(2008).
Structural, functional, and mutational analysis of the NblA protein provides insight into possible modes of interaction with the phycobilisome.
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J Biol Chem,
283,
30330-30340.
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PDB codes:
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T.Dammeyer,
E.Hofmann,
and
N.Frankenberg-Dinkel
(2008).
Phycoerythrobilin Synthase (PebS) of a Marine Virus: CRYSTAL STRUCTURES OF THE BILIVERDIN COMPLEX AND THE SUBSTRATE-FREE FORM.
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J Biol Chem,
283,
27547-27554.
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PDB codes:
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K.H.Zhao,
J.Zhang,
J.M.Tu,
S.Böhm,
M.Plöscher,
L.Eichacker,
C.Bubenzer,
H.Scheer,
X.Wang,
and
M.Zhou
(2007).
Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin beta-subunits.
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J Biol Chem,
282,
34093-34103.
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S.Böhm,
S.Endres,
H.Scheer,
and
K.H.Zhao
(2007).
Biliprotein chromophore attachment: chaperone-like function of the PecE subunit of alpha-phycoerythrocyanin lyase.
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J Biol Chem,
282,
25357-25366.
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A.Gaigalas,
T.Gallagher,
K.D.Cole,
T.Singh,
L.Wang,
and
Y.Z.Zhang
(2006).
A multistate model for the fluorescence response of R-phycoerythrin.
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Photochem Photobiol,
82,
635-644.
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G.Shen,
N.A.Saunée,
S.R.Williams,
E.F.Gallo,
W.M.Schluchter,
and
D.A.Bryant
(2006).
Identification and characterization of a new class of bilin lyase: the cpcT gene encodes a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta-subunit of phycocyanin in Synechococcus sp. PCC 7002.
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J Biol Chem,
281,
17768-17778.
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C.Six,
J.C.Thomas,
L.Thion,
Y.Lemoine,
F.Zal,
and
F.Partensky
(2005).
Two novel phycoerythrin-associated linker proteins in the marine cyanobacterium Synechococcus sp. strain WH8102.
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J Bacteriol,
187,
1685-1694.
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C.Steglich,
N.Frankenberg-Dinkel,
S.Penno,
and
W.R.Hess
(2005).
A green light-absorbing phycoerythrin is present in the high-light-adapted marine cyanobacterium Prochlorococcus sp. MED4.
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Environ Microbiol,
7,
1611-1618.
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C.Steglich,
A.F.Post,
and
W.R.Hess
(2003).
Analysis of natural populations of Prochlorococcus spp. in the northern Red Sea using phycoerythrin gene sequences.
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Environ Microbiol,
5,
681-690.
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N.Adir,
and
N.Lerner
(2003).
The crystal structure of a novel unmethylated form of C-phycocyanin, a possible connector between cores and rods in pycobilisomes.
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J Biol Chem,
278,
25926-25932.
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PDB code:
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T.Jiang,
J.P.Zhang,
W.R.Chang,
and
D.C.Liang
(2001).
Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome.
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Biophys J,
81,
1171-1179.
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PDB code:
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X.Q.Wang,
L.N.Li,
W.R.Chang,
J.P.Zhang,
L.L.Gui,
B.J.Guo,
and
D.C.Liang
(2001).
Structure of C-phycocyanin from Spirulina platensis at 2.2 A resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes.
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Acta Crystallogr D Biol Crystallogr,
57,
784-792.
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PDB code:
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H.Kikuchi,
H.Wako,
K.Yura,
M.Go,
and
M.Mimuro
(2000).
Significance of a two-domain structure in subunits of phycobiliproteins revealed by the normal mode analysis.
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Biophys J,
79,
1587-1600.
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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