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* Residue conservation analysis
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PDB id:
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Light harvesting protein
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Title:
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Isolation, crystallization, crystal structure analysis and refinement of constitutivE C-phycocyanin from the chromatically adapting cyanobacterium fremyella diplosiphon at 1.66 angstroms resolution
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Structure:
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C-phycocyanin (alpha subunit). Chain: a, k. Engineered: yes. C-phycocyanin (beta subunit). Chain: b, l. Engineered: yes
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Source:
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Fremyella diplosiphon. Organism_taxid: 1197. Organism_taxid: 1197
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Biol. unit:
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Dodecamer (from
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Resolution:
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Authors:
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M.Duerring,G.B.Schmidt,R.Huber
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Key ref:
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M.Duerring
et al.
(1991).
Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 A resolution.
J Mol Biol,
217,
577-592.
PubMed id:
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Date:
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11-Oct-90
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Release date:
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15-Jan-93
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PROCHECK
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Headers
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References
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J Mol Biol
217:577-592
(1991)
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PubMed id:
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Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 A resolution.
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M.Duerring,
G.B.Schmidt,
R.Huber.
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ABSTRACT
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Constitutive phycocyanin from cyanobacterium Fremyella diplosiphon (Calothrix
sp. PCC 7601) grown in green light, has been isolated and crystallized. The
crystals belong to the space group R3 with cell constants a = b = 180.26 A, c =
61.24 A, alpha = beta = 90 degrees, gamma = 120 degrees. The crystal structure
has been determined by Patterson search techniques using the molecular model of
C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. The asymmetric
unit of the crystal cell consists of two (alpha beta)-monomers related by a
local dyad. Three asymmetric units are arranged around a crystallographic triad
and form an (alpha beta)6-hexamer, the functional unit in the native antenna
rod. The initial structure has been refined in a cyclic manner by
energy-restrained crystallographic refinement and modelling until the
conventional crystallographic R-factor converged at 18.1% with data to a
resolution of 1.66 A. The molecular structure resembles closely the
C-phycocyanins of Mastigocladus laminosus and A. quadruplicatum. The
conformation and configuration of the alpha-84 and beta-84 chromophores is very
similar to the corresponding chromophores in the trimeric C-phycocyanin of M.
laminosus, whereas the beta-155 chromophore differs in configuration with
C(4)-Z, C(10)-Z and C(15)-Z compared to C(4)-Z, C(10)-Z, C(15)-Z,E. The
stereochemistry of the beta-155 chiral centres is C(2)-RC(3)-R and C(31)-S,
respectively, whereas alpha-84 and beta-84 have C(2)-RC(3)-R and C(31)-R. The
amino acid sequences of constitutive and inducible phycocyanin differ mainly in
residues located on the surface of the beta-subunits that mediate the
inter-hexameric contacts.
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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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PDB code:
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PDB code:
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Inaugural Article: finding important sites in protein sequences.
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PDB code:
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L.Li,
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PDB code:
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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
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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
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shown on the right.
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