1C7M

SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRIFICANS CYTOCHROME C552 IN THE REDUCED STATE

1C7M の概要

• エントリーDOI: 10.2210/pdb1c7m/pdb
• 分子名称: PROTEIN (CYTOCHROME C552), HEME C (2 entities in total)
• 機能のキーワード: electron transport, cytochrome c552, heme, redox states, isotope enrichment {15n}, nmr spectroscopy, solution structure
• 由来する生物種: Paracoccus denitrificans
• 細胞内の位置: Cell membrane; Single-pass membrane protein: P54820
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11172.48

構造登録者

Pristovsek, P.,Luecke, C.,Reincke, B.,Ludwig, B.,Rueterjans, H. (登録日: 2000-03-03, 公開日: 2000-07-19, 最終更新日: 2024-10-30)

主引用文献

Pristovsek, P.,Lucke, C.,Reincke, B.,Ludwig, B.,Ruterjans, H.
Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.
Eur.J.Biochem., 267:4205-4212, 2000

PubMed Abstract: In order to determine the solution structure of Paracoccus denitrificans cytochrome c552 by NMR, we cloned and isotopically labeled a 10.5-kDa soluble fragment (100 residues) containing the functional domain of the 18.2-kDa membrane-bound protein. Using uniformly 15N-enriched samples of cytochrome c552 in the reduced state, a variety of two-dimensional and three-dimensional heteronuclear double-resonance NMR experiments was employed to achieve complete 1H and 15N assignments. A total of 1893 distance restraints was derived from homonuclear 2D-NOESY and heteronuclear 3D-NOESY spectra; 1486 meaningful restraints were used in the structure calculations. After restrained energy minimization a family of 20 structures was obtained with rmsd values of 0.56 +/- 0. 10 A and 1.09 +/- 0.09 A for the backbone and heavy atoms, respectively. The overall topology is similar to that seen in previously reported models of this class of proteins. The global fold consists of two long helices at the N-terminus and C-terminus and three shorter helices surrounding the heme moiety; the helices are connected by well-defined loops. Comparison with the X-ray structure shows some minor differences in the positions of the Trp57 and Phe65 side-chain rings as well as the heme propionate groups.

PubMed: 10866825
DOI: 10.1046/j.1432-1327.2000.01456.x

実験手法

SOLUTION NMR