1s44

The structure and refinement of apocrustacyanin C2 to 1.6A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1.

spinqualitylabelsall models 1s44, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1s44 is a 2 chain structure with sequence from Homarus gammarus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: GOL, MPD, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRA1_HOMGA Binds the carotenoid astaxanthin (AXT) which provides the blue coloration to the carapace of the lobster. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The blue carotenoprotein alpha-crustacyanin of Homarus gammarus lobster carapace is comprised chemically of five 20 kDa subunits. Only two genes for the proteins have been isolated (J. B. C. Findlay, personal communication) and the five apoproteins fall into two sets of homologous proteins based on their chemical properties (CRTC, consisting of apoproteins C(1), C(2) and A(1), and CRTA, consisting of apoproteins A(2) and A(3)). The diffraction quality of apo C(2) has been improved from 2.2 to 1.3 A and its structure solved. The structure is compared with the A(1) and C(1) proteins determined at 1.4 A [Cianci et al. (2001), Acta Cryst. D57, 1219-1229] and 1.15 A, respectively [Gordon et al. (2001), Acta Cryst. D57, 1230-1237] and found to be very similar. Normalized B-factor difference plots per residue of different types were used to try to find chemically modified residues; none were found at these resolutions. It remains possible that the differences between the CRTC proteins result from differences in amidation. By comparison of a crystal grown with glycerol (studied at 1.6 A) and one grown without glycerol (studied at 1.3 A) it was seen that glycerol bound at the astaxanthin site. The structure and refinement of apocrustacyanin C2 to 1.3 A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1.,Habash J, Helliwell JR, Raftery J, Cianci M, Rizkallah PJ, Chayen NE, Nneji GA, Zagalsky PF Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):493-8. Epub 2004, Feb 25. PMID:14993674 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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