Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus.
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 H1 and H2 from the American lobster Homarus americanus are...
Published in: | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
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Language: | English |
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2012
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Online Access: | http://hdl.handle.net/11381/2509045 https://doi.org/10.1107/S1744309112026103 http://scripts.iucr.org/cgi-bin/paper?S1744309112026103 |
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ftunivparmairis:oai:air.unipr.it:11381/2509045 2024-04-14T08:11:15+00:00 Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. M. Ferrari E. Pincolini T. S. McClintock M. Rossle M. Cianci FOLLI, Claudia BERNI, Rodolfo M., Ferrari Folli, Claudia E., Pincolini T. S., Mcclintock M., Rossle Berni, Rodolfo M., Cianci 2012 http://hdl.handle.net/11381/2509045 https://doi.org/10.1107/S1744309112026103 http://scripts.iucr.org/cgi-bin/paper?S1744309112026103 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000307217700001 volume:F68 firstpage:846 lastpage:853 numberofpages:8 journal:ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS http://hdl.handle.net/11381/2509045 doi:10.1107/S1744309112026103 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84864871509 http://scripts.iucr.org/cgi-bin/paper?S1744309112026103 info:eu-repo/semantics/article 2012 ftunivparmairis https://doi.org/10.1107/S1744309112026103 2024-03-21T18:32:38Z 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 H1 and H2 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 H1 and H2 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. Article in Journal/Newspaper European lobster Archivio della ricerca dell'Università di Parma (CINECA IRIS) Acta Crystallographica Section F Structural Biology and Crystallization Communications 68 8 846 853 |
institution |
Open Polar |
collection |
Archivio della ricerca dell'Università di Parma (CINECA IRIS) |
op_collection_id |
ftunivparmairis |
language |
English |
description |
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 H1 and H2 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 H1 and H2 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. |
author2 |
M., Ferrari Folli, Claudia E., Pincolini T. S., Mcclintock M., Rossle Berni, Rodolfo M., Cianci |
format |
Article in Journal/Newspaper |
author |
M. Ferrari E. Pincolini T. S. McClintock M. Rossle M. Cianci FOLLI, Claudia BERNI, Rodolfo |
spellingShingle |
M. Ferrari E. Pincolini T. S. McClintock M. Rossle M. Cianci FOLLI, Claudia BERNI, Rodolfo Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. |
author_facet |
M. Ferrari E. Pincolini T. S. McClintock M. Rossle M. Cianci FOLLI, Claudia BERNI, Rodolfo |
author_sort |
M. Ferrari |
title |
Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. |
title_short |
Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. |
title_full |
Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. |
title_fullStr |
Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. |
title_full_unstemmed |
Structural characterization of recombinant crustacyanin subunits from the lobster Homarus americanus. |
title_sort |
structural characterization of recombinant crustacyanin subunits from the lobster homarus americanus. |
publishDate |
2012 |
url |
http://hdl.handle.net/11381/2509045 https://doi.org/10.1107/S1744309112026103 http://scripts.iucr.org/cgi-bin/paper?S1744309112026103 |
genre |
European lobster |
genre_facet |
European lobster |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000307217700001 volume:F68 firstpage:846 lastpage:853 numberofpages:8 journal:ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS http://hdl.handle.net/11381/2509045 doi:10.1107/S1744309112026103 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84864871509 http://scripts.iucr.org/cgi-bin/paper?S1744309112026103 |
op_doi |
https://doi.org/10.1107/S1744309112026103 |
container_title |
Acta Crystallographica Section F Structural Biology and Crystallization Communications |
container_volume |
68 |
container_issue |
8 |
container_start_page |
846 |
op_container_end_page |
853 |
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