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4ALO

STRUCTURE AND PROPERTIES OF H1 CRUSTACYANIN FROM LOBSTER HOMARUS AMERICANUS

Summary for 4ALO
Entry DOI10.2210/pdb4alo/pdb
Related1H91 1I4U 1OBQ 1OBU 1S2P
DescriptorH1 APOCRUSTACYANIN, (4S)-2-METHYL-2,4-PENTANEDIOL, SULFATE ION, ... (5 entities in total)
Functional Keywordstransport protein, chromophore binding protein, bathochromic shift, astaxanthin, colouration, recombinant carotenoproteins, carapace
Biological sourceHOMARUS AMERICANUS (AMERICAN LOBSTER)
Cellular locationSecreted, extracellular space: P80029
Total number of polymer chains2
Total formula weight42528.63
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 citationFerrari, 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: 22869108
DOI: 10.1107/S1744309112026103
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.37 Å)
Structure validation

227561

数据于2024-11-20公开中

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