1h91
From Proteopedia
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Revision as of 13:27, 30 October 2007
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THE CRYSTAL STRUCTURE OF LOBSTER APOCRUSTACYANIN A1 USING SOFTER X-RAYS.
Overview
The molecular basis of the camouflage colouration of marine crustacea is, often provided by carotenoproteins. The blue colour of the lobster, carapace, for example, is intricately associated with a, multimacromolecular 16-mer complex of protein subunits each with a bound, astaxanthin molecule. The protein subunits of crustacyanin fall into two, distinct subfamilies, CRTC and CRTA. Here, the crystal structure solution, of the A(1) protein of the CRTC subfamily is reported. The problematic, nature of the structure solution of the CRTC proteins (both C(1) and A(1)), warranted consideration and the development of new approaches. Three, putative disulfides per protein subunit were likely to exist based on, molecular-homology modelling against known lipocalin protein structures., With two such ... [(full description)]
About this Structure
1H91 is a [Single protein] structure of sequence from [Homarus gammarus] with MPD as [ligand]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [OCA].
Reference
Structure of lobster apocrustacyanin A1 using softer X-rays., Cianci M, Rizkallah PJ, Olczak A, Raftery J, Chayen NE, Zagalsky PF, Helliwell JR, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1219-29. Epub 2001, Aug 23. PMID:11526313
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