1BFX

THE SOLUTION NMR STRUCTURE OF THE B FORM OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, MINIMIZED AVERAGE STRUCTURE

1BFX の概要

• エントリーDOI: 10.2210/pdb1bfx/pdb
• 分子名称: CYTOCHROME B5, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: electron transport, cytochrome b5, protein recognition, electron transfer, solution structure, paramagnetic nmr
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side: P00173
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11976.99

構造登録者

Arnesano, F.,Banci, L.,Bertini, I.,Felli, I.C. (登録日: 1998-05-23, 公開日: 1998-08-12, 最終更新日: 2024-05-22)

主引用文献

Arnesano, F.,Banci, L.,Bertini, I.,Felli, I.C.,Koulougliotis, D.
Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications.
Eur.J.Biochem., 260:347-354, 1999

PubMed Abstract: Cytochrome b5 in solution has two isomers (A and B) differing by a 180 degrees rotation of the protoporphyrin IX plane around the axis defined by the alpha and gamma meso protons. Homonuclear and heteronuclear NMR spectroscopy has been employed in order to solve the solution structure of the minor (B) form of the oxidized state of the protein and to probe its backbone dynamics in the microsecond--ms timescale in both oxidation states. A family of 40 conformers has been obtained using 1302 meaningful NOEs and 220 pseudocontact shifts and is characterized by high quality and good resolution (rmsd to the mean structure of 0.055 +/- 0.009 nm and 0.103 +/- 0.011 nm for backbone and heavy atoms, respectively). Extensive comparisons of the structural and dynamics changes associated with the A-to-B form interconversion for both oxidation states were subsequently performed. Propionate 6 experiences a redox-state-dependent reorientation as does propionate 7 in the A form. Significant insights are obtained into the role of the protein frame for efficient biological function and backbone mobility is proposed to be one of the factors that could control the reduction potential of the heme.

PubMed: 10095768
DOI: 10.1046/j.1432-1327.1999.00167.x

実験手法

SOLUTION NMR