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The molecular basis of the coloration mechanism in lobster shell: β-Crustacyanin at 3.2-Å resolution
TLDR
Lobster has clearly evolved an intricate structural mechanism for the coloration of its shell using AXT and a bathochromic shift mechanism, and the three-dimensional structure of β-CR has identified the protein contacts and structural alterations needed for the AXT color regulation mechanism. Expand
Unravelling the structural chemistry of the colouration mechanism in lobster shell.
TLDR
A review of progress concentrating on recent results but set in the context of more than 50 years of work is presented, including the first observation of single-crystal diffraction of the full 'alpha-crustacyanin' complex comprising 16 protein subunits and 16 bound AXT molecules at 5 A resolution. 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.
The previously unknown crystal structure of the C(1) subunit of the carotenoid-binding protein alpha-crustacyanin has been determined using the anomalous scattering available at 1.77 A wavelength toExpand
CAROTENOPROTEINS IN INVERTEBRATES
TLDR
Although the relationship between the carotenoid and the remainder of the complex may in these cases not appear to be stoichiometric, it often shows some evidence of selectivity. Expand
Invertebrate carotenoproteins.
Carotenoid-Protein Complexes
Abstract A survey of carotenoid-protein complexes is presented. Distinction is made between astaxanthin-proteins in which the absorption band of the carotenoid is unaltered in shape, andExpand
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.
TLDR
The complete sequence has been determined for the C1 subunit of crustacyanin, an astaxanthin-binding protein from the carapace of the lobster Homarus gammarus, and a tentative model for the dimer, beta-crustacyanIn, formed between the two subunits with their associated carotenoid ligands, is discussed. Expand
Studies on the quaternary structure of the lobster exoskeleton carotenoprotein, crustacyanin.
TLDR
Although each apoprotein has the ability to form the dimer, β-crustacyanin, on combination with astaxanthin, association between pairs of apoproteins, one from each set, occurs more readily. Expand
beta-Crustacyanin, the blue-purple carotenoprotein of lobster carapace: consideration of the bathochromic shift of the protein-bound astaxanthin.
  • P. F. Zagalsky
  • Chemistry, Medicine
  • Acta crystallographica. Section D, Biological…
  • 1 August 2003
TLDR
This mini review enlarges on the original analysis and conclusions of Cianci et al. and indicates that extension of conjugation by coplanarization of the beta-ionone rings with the polyene chain and polarization resulting from hydrogen bonding at the C(4) and C( 4') keto groups may be mainly responsible for the bathochromic shift. Expand
Apocrustacyanin C(1) crystals grown in space and on earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisons.
TLDR
It is concluded that the electron-density maps of the protein and the bound waters are found to be better overall for the structures of apocrustacyanin C(1) studied from the space-grown crystal compared with those from the earth- grown crystal, even though both crystals were grown using vapour-diffusion crystal-growth geometry. Expand
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