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.

1S44 の概要

• エントリーDOI: 10.2210/pdb1s44/pdb
• 関連するPDBエントリー: 1s2p
• 分子名称: Crustacyanin A1 subunit, SULFATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• 機能のキーワード: crustacyanin, refinement, post-translational modifications, glycerol, protein binding
• 由来する生物種: Homarus gammarus (European lobster)
• 細胞内の位置: Secreted, extracellular space: P58989
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41636.63

構造登録者

Habash, J.,Helliwell, J.R.,Raftery, J.,Cianci, M.,Rizkallah, P.J.,Chayen, N.E.,Nneji, G.A.,Zagalsky, P.F. (登録日: 2004-01-15, 公開日: 2004-04-27, 最終更新日: 2024-11-20)

主引用文献

Habash, J.,Helliwell, J.R.,Raftery, J.,Cianci, M.,Rizkallah, P.J.,Chayen, N.E.,Nneji, G.A.,Zagalsky, P.F.
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.
Acta Crystallogr.,Sect.D, 60:493-498, 2004

PubMed Abstract: 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.

PubMed: 14993674
DOI: 10.1107/S090744490400037X

実験手法

X-RAY DIFFRACTION (1.6 Å)