Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin
The complete sequence has been determined for the C 1 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, A 2 and to plasma retinol‐binding protein. Th...
Published in: | European Journal of Biochemistry |
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crwiley:10.1111/j.1432-1033.1991.tb16340.x 2024-06-23T07:53:33+00:00 Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin KEEN, Jeffrey N. CACERES, Isabel ELIOPOULOS, Elias E. ZAGALSKY, Peter F. FINDLAY, John B. C. 1991 http://dx.doi.org/10.1111/j.1432-1033.1991.tb16340.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1991.tb16340.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1991.tb16340.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 202, issue 1, page 31-40 ISSN 0014-2956 1432-1033 journal-article 1991 crwiley https://doi.org/10.1111/j.1432-1033.1991.tb16340.x 2024-06-13T04:22:22Z The complete sequence has been determined for the C 1 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, A 2 and to plasma retinol‐binding protein. The tertiary structure of the C 1 subunit has been modelled on that derived for the A 2 subunit from the coordinates of retinol‐binding protein. Residues lining the putative binding cavities and at the putative carotenoid binding sites of the two subunits are highly conserved. The carotenoid environments are characterized by a preponderance of aromatic and polar residues and the absence of charged side‐chains. A tentative model for the dimer, β‐crustacyanin, formed between the two subunits with their associated carotenoid ligands, is discussed. The model is based on the crystal structure of the dimer of bilin‐binding protein, a member of the same superfamily. This structure has enabled us to examine mechanisms for the bathochromic spectral shift of the protein‐bound carotenoid and to identify likely contact regions between dimers in octameric α‐crustacyanin. Article in Journal/Newspaper Homarus gammarus Wiley Online Library European Journal of Biochemistry 202 1 31 40 |
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Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
The complete sequence has been determined for the C 1 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, A 2 and to plasma retinol‐binding protein. The tertiary structure of the C 1 subunit has been modelled on that derived for the A 2 subunit from the coordinates of retinol‐binding protein. Residues lining the putative binding cavities and at the putative carotenoid binding sites of the two subunits are highly conserved. The carotenoid environments are characterized by a preponderance of aromatic and polar residues and the absence of charged side‐chains. A tentative model for the dimer, β‐crustacyanin, formed between the two subunits with their associated carotenoid ligands, is discussed. The model is based on the crystal structure of the dimer of bilin‐binding protein, a member of the same superfamily. This structure has enabled us to examine mechanisms for the bathochromic spectral shift of the protein‐bound carotenoid and to identify likely contact regions between dimers in octameric α‐crustacyanin. |
format |
Article in Journal/Newspaper |
author |
KEEN, Jeffrey N. CACERES, Isabel ELIOPOULOS, Elias E. ZAGALSKY, Peter F. FINDLAY, John B. C. |
spellingShingle |
KEEN, Jeffrey N. CACERES, Isabel ELIOPOULOS, Elias E. ZAGALSKY, Peter F. FINDLAY, John B. C. Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin |
author_facet |
KEEN, Jeffrey N. CACERES, Isabel ELIOPOULOS, Elias E. ZAGALSKY, Peter F. FINDLAY, John B. C. |
author_sort |
KEEN, Jeffrey N. |
title |
Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin |
title_short |
Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin |
title_full |
Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin |
title_fullStr |
Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin |
title_full_unstemmed |
Complete sequence and model for the C 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C 1 and A 2 subunits with astaxanthin |
title_sort |
complete sequence and model for the c 1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the c 1 and a 2 subunits with astaxanthin |
publisher |
Wiley |
publishDate |
1991 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1991.tb16340.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1991.tb16340.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1991.tb16340.x |
genre |
Homarus gammarus |
genre_facet |
Homarus gammarus |
op_source |
European Journal of Biochemistry volume 202, issue 1, page 31-40 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1991.tb16340.x |
container_title |
European Journal of Biochemistry |
container_volume |
202 |
container_issue |
1 |
container_start_page |
31 |
op_container_end_page |
40 |
_version_ |
1802645267664601088 |