Abstract
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 (lambda(max) 472 nm in hexane), the well-known color of cooked lobster, to slate blue in the protein-bound live lobster state (lambda(max) 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(1) 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 beta-CR holo complex, that is an A(1) with A(3) subunit assembly including two bound AXT molecules. We have thereby determined the structure of the A(3) molecule de novo. 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 beta-CR has identified the protein contacts and structural alterations needed for the AXT color regulation mechanism.