Complete sequence and model for the C1 subunit of the carotenoprotein, crustacyanin, and model for the dimer, beta-crustacyanin, formed from the C1 and A2 subunits with astaxanthin.

@article{Keen1991CompleteSA,
  title={Complete sequence and model for the C1 subunit of the carotenoprotein, crustacyanin, and model for the dimer, beta-crustacyanin, formed from the C1 and A2 subunits with astaxanthin.},
  author={J. Keen and I. C{\'a}ceres and E. Eliopoulos and P. F. Zagalsky and J. Findlay},
  journal={European journal of biochemistry},
  year={1991},
  volume={202 1},
  pages={
          31-40
        }
}
The complete sequence has been determined for the C1 subunit of crustacyanin, an astaxanthin-binding protein from the carapace of the lobster Homarus gammarus (L.). The polypeptide, 181 residues long, is similar (38% identity) to the other main subunit, A2 and to plasma retinol-binding protein. The tertiary structure of the C1 subunit has been modelled on that derived for the A2 subunit from the coordinates of retinol-binding protein. Residues lining the putative binding cavities and at the… Expand
The C1 subunit of alpha-crustacyanin: the de novo phasing of the crystal structure of a 40 kDa homodimeric protein using the anomalous scattering from S atoms combined with direct methods.
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Crustacyanin, the lobster carapace astaxanthin-protein: effects of modification of tyrosine residues of apocrustacyanin with tetranitromethane on the ability of the protein to reconstitute with astaxanthin
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A study of protein-carotenoid interactions in the astaxanthin-protein crustacyanin by absorption and Stark spectroscopy; evidence for the presence of three spectrally distinct species.
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This paper describes the structure solution of CRTC in the form of the A(1) dimer based on use of softer X-rays, which can now be used as a search motif in the structural studies of the oligomeric forms alpha- and beta-crustacyanins, which contain bound astaxanthin molecules. Expand
The quaternary structure of the lobster carapace carotenoprotein, crustacyanin: Studies using cross-linking agents
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TLDR
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Apocrustacyanin A1 from the lobster carotenoprotein alpha-crustacyanin: crystallization and initial X-ray analysis involving softer X-rays.
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The A1 subunit of the carotenoprotein alpha-crustacyanin, isolated from lobster carapace, has been crystallized using the vapour-diffusion method and an approach based on the S atoms is being undertaken involving softer X-rays at the SRS, Daresbury. Expand
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It is beginning to appear as though this superfamily of proteins, characterized by a similar gross structural framework, may be further subdivided into interrelated subclasses, as well as the putative identification of side-chains which line the binding cavity. Expand
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Crustacyanin, the blue carapace pigment of the common lobster Homarus gammarus (L.), has been purified and crystallized. This chromoprotein has a minimum molecular weight of 36 000 based on theExpand
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TLDR
Interestingly the overall three‐dimensional fold of the insecticyanin subunit shows remarkable similarity to the structural motifs of bovine beta‐lactoglobulin and the human serum retinol‐binding protein. Expand
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