1YFC

Solution nmr structure of a yeast iso-1-ferrocytochrome C

1YFC の概要

• エントリーDOI: 10.2210/pdb1yfc/pdb
• 分子名称: YEAST ISO-1-FERROCYTOCHROME C, HEME C (2 entities in total)
• 機能のキーワード: ferrocytochrome, mitochondrion, electron transport, respiratory chain, methylation
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion intermembrane space: P00044
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12718.35

構造登録者

Baistrocchi, P.,Banci, L.,Bertini, I.,Turano, P.,Bren, K.L.,Gray, H.B. (登録日: 1996-08-08, 公開日: 1997-03-12, 最終更新日: 2021-11-03)

主引用文献

Baistrocchi, P.,Banci, L.,Bertini, I.,Turano, P.,Bren, K.L.,Gray, H.B.
Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c.
Biochemistry, 35:13788-13796, 1996

PubMed Abstract: Two-dimensional 1H NMR spectra of Saccharomyces cerevisiae reduced iso-1-cytochrome c have been used to confirm and slightly extend the assignment available in the literature. 1702 NOESY cross-peaks have been assigned, and their intensities have been measured. Through the program DIANA and related protocols (Güntert, 1992), a solution structure has been obtained by using 1442 meaningful NOEs and 13 hydrogen-bond constraints. The RMSD values with respect to the mean structure for the backbone and all heavy atoms for a family of 20 structures are 0.61 +/- 0.09 and 0.98 +/- 0.09 A, the average target function value being as small as 0.57 A2. The larger number of slowly exchanging amide NHs observed in this system compared to that observed in the cyanide derivative of oxidized Ala 80 cytochrome c suggests that the oxidized form is much more flexible and that the backbone protons are more solvent accessible. Comparison of the present structure with the crystal structures of reduced yeast cytochrome c and of the complex between cytochrome c peroxidase and oxidized yeast cytochrome c reveals substantial similarity among the backbone conformations but differences in the residues located in the region of protein-protein interaction. Interestingly, in solution the peripheral residues involved in the interaction with cytochrome c peroxidase are on average closer to the position found in the crystal structure of the complex than to the solid state structure of the isolated reduced from.

PubMed: 8901521
DOI: 10.1021/bi961110e

実験手法

SOLUTION NMR