1J0Q

Solution Structure of Oxidized Bovine Microsomal Cytochrome b5 mutant V61H

1J0Q の概要

• エントリーDOI: 10.2210/pdb1j0q/pdb
• 分子名称: cytochrome b5, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: helix, beta, electron transport
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side: P00171
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10130.88

構造登録者

Wu, H.,Huang, Z.,Cao, C.,Zhang, Q.,Wang, Y.-H.,Ma, J.-B.,Xue, L.-L. (登録日: 2002-11-20, 公開日: 2003-08-12, 最終更新日: 2023-12-27)

主引用文献

Cao, C.,Zhang, Q.,Xue, L.-L.,Ma, J.,Wang, Y.-H.,Wu, H.,Huang, Z.-X.
The solution structure of the oxidized bovine microsomal cytochrome b5 mutant V61H
Biochem.Biophys.Res.Commun., 307:600-609, 2003

PubMed Abstract: Using 1488 NOE constraints, 19 stereo-specific assignments, 13 pairs of H-bond constraints, and 140 pseudo-contact shift constraints, a family of 35 structures of bovine microsomal cytochrome b(5) mutant V61H has been obtained through the program PSEUDYANA. The family has been further refined by restrained energy minimization to give a family of final structures. The RMSD values of final structures with respect to the average structure are 0.45+/-0.11 and 0.96+/-0.10A for backbone and heavy atoms, respectively. The final Deltachi(ax) and Deltachi(rh) values are 2.34 x 10(-32) and -0.67 x 10(-32)m(3), respectively. The comparisons between the solution structures of mutant V61H and WT cytochrome b(5), and X-ray structure of the mutant V61H show that the global folding of the molecule in solution is unchanged and the side-chain of His61 deviates from the heme pocket and extends into the solvent like in its crystal structure. However, the helices around the heme pocket undergo outward global displacement while their local conformations are well maintained. Meanwhile, the heme ring shows a little off the heme pocket, which accounts for the lower stability of the mutant. Additionally, the axial ligand rings counterclockwise rotate around His39 N-Fe axis due to the mutation, which is confirmed by variation of the hyperfine shifts of the heme protons of V61H compared to those of WT cytochrome b(5).

PubMed: 12893266
DOI: 10.1016/S0006-291X(03)01225-7

実験手法

SOLUTION NMR