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PDBsum entry 1vrn
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Photosynthesis
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PDB id
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1vrn
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Contents |
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332 a.a.
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258 a.a.
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273 a.a.
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323 a.a.
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* Residue conservation analysis
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PDB id:
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Photosynthesis
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Title:
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Photosynthetic reaction center blastochloris viridis (atcc)
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Structure:
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Photosynthetic reaction center cytochromE C subunit. Chain: c. Synonym: cytochrome c558/c559. Reaction center protein h chain. Chain: h. Synonym: photosynthetic reaction center h subunit. Reaction center protein l chain. Chain: l. Synonym: photosynthetic reaction center l subunit.
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Source:
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Blastochloris viridis. Organism_taxid: 1079. Organism_taxid: 1079
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Biol. unit:
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Tetramer (from
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Resolution:
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2.20Å
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R-factor:
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0.191
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R-free:
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0.212
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Authors:
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R.H.G.Baxter,B.-L.Seagle,J.R.Norris
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Key ref:
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R.H.Baxter
et al.
(2005).
Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark.
Acta Crystallogr D Biol Crystallogr,
61,
605-612.
PubMed id:
DOI:
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Date:
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23-Feb-05
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Release date:
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22-Mar-05
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Supersedes:
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PROCHECK
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Headers
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References
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P07173
(CYCR_BLAVI) -
Photosynthetic reaction center cytochrome c subunit from Blastochloris viridis
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Seq:
Struc:
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356 a.a.
332 a.a.
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P06008
(RCEH_BLAVI) -
Reaction center protein H chain from Blastochloris viridis
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Seq:
Struc:
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258 a.a.
258 a.a.*
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DOI no:
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Acta Crystallogr D Biol Crystallogr
61:605-612
(2005)
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PubMed id:
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Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark.
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R.H.Baxter,
B.L.Seagle,
N.Ponomarenko,
J.R.Norris.
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ABSTRACT
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The structure of the Blastochloris viridis photosynthetic reaction center has
been determined at 100 K by flash-freezing crystals. A data set to 2.2 A
resolution provides a well determined model of the wild-type protein. Of
particular interest are the position, occupancy and heterogeneity of the
Q(B)-binding site. Data were also collected from a crystal frozen immediately
after illumination. The data support predominant binding of Q(B) in the proximal
position in both the neutral and charge-separated states.
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Selected figure(s)
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Figure 1.
Figure 1
Simulated-annealing F[o] - F[c] (a) and refined 2F[o] - F[c] (b) electron density for Q[B]
in its active site. Maps contoured at 1.5 [sigma] and 1.0 [sigma] ,
respectively. The alternate model for the quinone is shown in yellow. Figs. 1 and 2 were
produced using PyMOL (DeLano, 2002 [DeLano, W. L. (2002). The PyMOL Molecular
Graphics System, http://www.pymol.org.]-[bluearr.gif] ).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
605-612)
copyright 2005.
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Figure was
selected
by an automated process.
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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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L.Li,
D.Mustafi,
Q.Fu,
V.Tereshko,
D.L.Chen,
J.D.Tice,
and
R.F.Ismagilov
(2006).
Nanoliter microfluidic hybrid method for simultaneous screening and optimization validated with crystallization of membrane proteins.
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Proc Natl Acad Sci U S A,
103,
19243-19248.
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PDB code:
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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
code is
shown on the right.
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