{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T05:01:01Z","timestamp":1790830861669,"version":"4.1.0"},"reference-count":35,"publisher":"National Academy of Sciences","issue":"15","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,7,23]]},"abstract":"<jats:p>\n                    The binding of the carotenoid astaxanthin (AXT) in the protein multimacromolecular complex crustacyanin (CR) is responsible for the blue coloration of lobster shell. The structural basis of the bathochromic shift mechanism has long been elusive. A change in color occurs from the orange red of the unbound dilute AXT (\u03bb\n                    <jats:sub>max<\/jats:sub>\n                    472 nm in hexane), the well-known color of cooked lobster, to slate blue in the protein-bound live lobster state (\u03bb\n                    <jats:sub>max<\/jats:sub>\n                    632 nm in CR). Intriguingly, extracted CR becomes red on dehydration and on rehydration goes back to blue. Recently, the innovative use of softer x-rays and xenon derivatization yielded the three-dimensional structure of the A\n                    <jats:sub>1<\/jats:sub>\n                    apoprotein subunit of CR, confirming it as a member of the lipocalin superfamily. That work provided the molecular replacement search model for a crystal form of the \u03b2-CR holo complex, that is an A\n                    <jats:sub>1<\/jats:sub>\n                    with A\n                    <jats:sub>3<\/jats:sub>\n                    subunit assembly including two bound AXT molecules. We have thereby determined the structure of the A\n                    <jats:sub>3<\/jats:sub>\n                    molecule\n                    <jats:italic>de novo<\/jats:italic>\n                    . Lobster has clearly evolved an intricate structural mechanism for the coloration of its shell using AXT and a bathochromic shift. Blue\/purple AXT proteins are ubiquitous among invertebrate marine animals, particularly the Crustacea. The three-dimensional structure of \u03b2-CR has identified the protein contacts and structural alterations needed for the AXT color regulation mechanism.\n                  <\/jats:p>","DOI":"10.1073\/pnas.152088999","type":"journal-article","created":{"date-parts":[[2002,7,28]],"date-time":"2002-07-28T18:26:28Z","timestamp":1027880788000},"page":"9795-9800","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":200,"title":["The molecular basis of the coloration mechanism in lobster shell: \u03b2-Crustacyanin at 3.2-\u212b resolution"],"prefix":"10.1073","volume":"99","author":[{"given":"Michele","family":"Cianci","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre J.","family":"Rizkallah","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrzej","family":"Olczak","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Raftery","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naomi E.","family":"Chayen","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter F.","family":"Zagalsky","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John R.","family":"Helliwell","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom; Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, United Kingdom; Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom; and Department of Molecular Biology and Biochemistry, Royal Holloway College, University of London, Egham, Surrey TW20 OEX, United..."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2002,7,15]]},"reference":[{"key":"e_1_3_4_1_2","first-page":"249","volume":"95","author":"Wald G","year":"1948","unstructured":"G Wald, N Nathanson, W P Jencks, E Tarr Biol Bull (Woods Hole, MA) 95, 249\u2013250 (1948).","journal-title":"Biol Bull (Woods Hole, MA)"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1021\/bi00842a043","volume":"7","author":"Buchwald M","year":"1968","unstructured":"M Buchwald, W P Jencks Biochemistry 7, 844\u2013859 (1968).","journal-title":"Biochemistry"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/0005-2795(79)90496-3","volume":"576","author":"Salares V R","year":"1979","unstructured":"V R Salares, N M Young, H J Bernstein, P R Carey Biochim Biophys Acta 576, 176\u2013191 (1979).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1351\/pac199769102075","volume":"69","author":"Britton G","year":"1997","unstructured":"G Britton, R J Weesie, D Askin, J D Warburton, L Gallardo-Guerrero, F J Jansen, H J M de Groot, J Lugtenburg, J-P Cornard, J-C Merlin Pure Appl Chem 69, 2075\u20132084 (1997).","journal-title":"Pure Appl Chem"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"2085","DOI":"10.1351\/pac199769102085","volume":"69","author":"Weesie R J","year":"1997","unstructured":"R J Weesie, R Verel, F J H M Jansen, G Britton, J Lugtenburg, H J M de Groot Pure Appl Chem 69, 2085\u20132090 (1997).","journal-title":"Pure Appl Chem"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/S0167-4838(00)00242-9","volume":"1544","author":"Krawczyk S","year":"2001","unstructured":"S Krawczyk, G Britton Biochim Biophys Acta 1544, 301\u2013310 (2001).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1111\/j.1432-1033.1991.tb16340.x","volume":"202","author":"Keen J N","year":"1991","unstructured":"J N Keen, I Caceres, E E Eliopoulos, P F Zagalsky, J B C Findlay Eur J Biochem 202, 31\u201340 (1991).","journal-title":"Eur J Biochem"},{"key":"e_1_3_4_8_2","first-page":"55","volume":"56","author":"Quarmby R","year":"1977","unstructured":"R Quarmby, D A Norden, P F Zagalsky, H J Ceccaldi, R Daumas Comp Biochem Physiol 56B, 55\u201361 (1977).","journal-title":"Comp Biochem Physiol"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1126\/science.289.5480.733","volume":"289","author":"Bourne H R","year":"2000","unstructured":"H R Bourne, E C Meng Science 289, 733\u2013745 (2000).","journal-title":"Science"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1126\/science.289.5480.739","volume":"289","author":"Palczewski K","year":"2000","unstructured":"K Palczewski, T Kumasaka, T Hori, C A Behnke, H Motoshima, B A Fox, I Le Trong, D C Teller, T Okada, R E Stenkamp, et al. 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