1NEW

Cytochrome C551.5, NMR

「1CFO」から置き換えられました 「2NEW」から置き換えられました

1NEW の概要

• エントリーDOI: 10.2210/pdb1new/pdb
• 分子名称: CYTOCHROME C551.5, HEME C (2 entities in total)
• 機能のキーワード: electron transport, cytochrome, multiheme cytochrome, cytochrome c7
• 由来する生物種: Desulfuromonas acetoxidans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9135.82

構造登録者

Assfalg, M.,Banci, L.,Bertini, I.,Bruschi, M.,Turano, P. (登録日: 1998-02-10, 公開日: 1998-04-29, 最終更新日: 2024-10-30)

主引用文献

Assfalg, M.,Banci, L.,Bertini, I.,Bruschi, M.,Turano, P.
800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.
Eur.J.Biochem., 256:261-270, 1998

PubMed Abstract: The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein, composed of 68 amino acids, contains three paramagnetic heme moieties, each with one unpaired electron. The largely distributed paramagnetism broadens the lines in several protein parts. The structure is now relatively well resolved all over the backbone by the use of 1315 meaningful NOEs and 90 pseudocontact shifts. The statistical analysis of the structure indicates its satisfactory quality. The protein-fold is quite similar to that of the analogous four-heme cytochromes c3 for those parts which can be considered homologous. The solvent accessibility and the electrostatic potential surfaces surrounding the three hemes have been analyzed in terms of their reduction potentials. The resulting magnetic susceptibility anisotropy data obtained from pseudocontact shifts are analyzed in terms of structural data.

PubMed: 9760163
DOI: 10.1046/j.1432-1327.1998.2560261.x

実験手法

SOLUTION NMR