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1cpc

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[[Image:1cpc.gif|left|200px]]
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{{STRUCTURE_1cpc| PDB=1cpc | SCENE= }}
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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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===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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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 1899708 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1899708}}
==About this Structure==
==About this Structure==
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[[Category: Schmidt, G B.]]
[[Category: Schmidt, G B.]]
[[Category: Light harvesting protein]]
[[Category: Light harvesting protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:03:26 2008''

Revision as of 18:03, 30 June 2008

Image:1cpc.png

Template:STRUCTURE 1cpc

ISOLATION, CRYSTALLIZATION, CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF CONSTITUTIVE C-PHYCOCYANIN FROM THE CHROMATICALLY ADAPTING CYANOBACTERIUM FREMYELLA DIPLOSIPHON AT 1.66 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1899708

About this Structure

1CPC is a Protein complex structure of sequences from Fremyella diplosiphon. Full crystallographic information is available from OCA.

Reference

Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 A resolution., Duerring M, Schmidt GB, Huber R, J Mol Biol. 1991 Feb 5;217(3):577-92. PMID:1899708

Page seeded by OCA on Mon Jun 30 21:03:26 2008

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