1s2p
From Proteopedia
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'''The structure and refinement of apocrustacyanin C2 to 1.3A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1''' | '''The structure and refinement of apocrustacyanin C2 to 1.3A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1''' | ||
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[[Category: Rizkallah, P J.]] | [[Category: Rizkallah, P J.]] | ||
[[Category: Zakalsky, P F.]] | [[Category: Zakalsky, P F.]] | ||
| - | [[Category: | + | [[Category: Apocrustacyanin]] |
| - | [[Category: | + | [[Category: Post-translational modification]] |
| - | [[Category: | + | [[Category: X-ray refinement]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:13:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:13, 3 May 2008
The structure and refinement of apocrustacyanin C2 to 1.3A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1
Overview
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.
About this Structure
1S2P is a Single protein structure of sequence from Homarus gammarus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 08:13:23 2008
