1gka

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spinqualitylabelsall models 1gka, resolution 3.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE MOLECULAR BASIS OF THE COLORATION MECHANISM IN LOBSTER SHELL. BETA-CRUSTACYANIN AT 3.2 A RESOLUTION

Overview

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 ... [(full description)]

About this Structure

1GKA is a [Protein complex] structure of sequences from [Homarus gammarus] with AXT, D12, TRS and EPE as [ligands]. Structure known Active Site: AX1. Full crystallographic information is available from [OCA].

Reference

The molecular basis of the coloration mechanism in lobster shell: beta-crustacyanin at 3.2-A resolution., Cianci M, Rizkallah PJ, Olczak A, Raftery J, Chayen NE, Zagalsky PF, Helliwell JR, Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9795-800. Epub 2002 Jul 15. PMID:12119396

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