4ALO
STRUCTURE AND PROPERTIES OF H1 CRUSTACYANIN FROM LOBSTER HOMARUS AMERICANUS
Summary for 4ALO
Entry DOI | 10.2210/pdb4alo/pdb |
Related | 1H91 1I4U 1OBQ 1OBU 1S2P |
Descriptor | H1 APOCRUSTACYANIN, (4S)-2-METHYL-2,4-PENTANEDIOL, SULFATE ION, ... (5 entities in total) |
Functional Keywords | transport protein, chromophore binding protein, bathochromic shift, astaxanthin, colouration, recombinant carotenoproteins, carapace |
Biological source | HOMARUS AMERICANUS (AMERICAN LOBSTER) |
Cellular location | Secreted, extracellular space: P80029 |
Total number of polymer chains | 2 |
Total formula weight | 42528.63 |
Authors | Ferrari, M.,Folli, C.,Pincolini, E.,Mcclintock, T.S.,Roessle, M.,Berni, R.,Cianci, M. (deposition date: 2012-03-05, release date: 2012-08-08, Last modification date: 2024-11-20) |
Primary citation | Ferrari, M.,Folli, C.,Pincolini, E.,Mcclintock, T.S.,Rossle, M.,Berni, R.,Cianci, M. Structural Characterization of Recombinant Crustacyanin Subunits from the Lobster Homarus Americanus. Acta Crystallogr.,Sect.F, 68:846-, 2012 Cited by PubMed Abstract: Crustacean crustacyanin proteins are linked to the production and modification of carapace colour, with direct implications for fitness and survival. Here, the structural and functional properties of the two recombinant crustacyanin subunits H(1) and H(2) from the American lobster Homarus americanus are reported. The two subunits are structurally highly similar to the corresponding natural apo crustacyanin CRTC and CRTA subunits from the European lobster H. gammarus. Reconstitution studies of the recombinant crustacyanin proteins H(1) and H(2) with astaxanthin reproduced the bathochromic shift of 85-95 nm typical of the natural crustacyanin subunits from H. gammarus in complex with astaxanthin. Moreover, correlations between the presence of crustacyanin genes in crustacean species and the resulting carapace colours with the spectral properties of the subunits in complex with astaxanthin confirmed this genotype-phenotype linkage. PubMed: 22869108DOI: 10.1107/S1744309112026103 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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