1SH4

Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H

1SH4 の概要

• エントリーDOI: 10.2210/pdb1sh4/pdb
• 関連するPDBエントリー: 1nx7
• NMR情報: BMRB: 6131
• 分子名称: Cytochrome b5, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: five helix, five sheet, heme ring, 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.,Zhang, Q. (登録日: 2004-02-25, 公開日: 2004-08-10, 最終更新日: 2024-05-29)

主引用文献

Zhang, Q.,Cao, C.,Wang, Z.Q.,Wang, Y.H.,Wu, H.,Huang, Z.X.
The comparative study on the solution structures of the oxidized bovine microsomal cytochrome b5 and mutant V45H
Protein Sci., 13:2161-2169, 2004

PubMed Abstract: A comparative study on the solution structures of bovine microsomal cytochrome b5 (Tb5) and the mutant V45H has been achieved by 1D and 2D 1H-NMR spectroscopy to clarify the differences in the solution conformations between these two proteins. The results reveal that the global folding of the V45H mutant in solution is unchanged, but the subtle changes exist in the orientation of the axial ligand His39, and heme vinyl groups. The side chain of His45 in V45H mutant extends to the outer edge of the heme pocket leaving a cavity at the site originally occupied by the inner methyl group of Val45 residue. In addition, the imidazole ring of axial ligand His39 rotates counterclockwise by approximately 3 degrees around the His-Fe-His axis, and the 4-heme vinyl group turns to the space vacated by the removed side chain due to the mutation. Furthermore, the helix III of the heme pocket undergoes outward displacement, while the linkage between helix II and III is shifted leftward. These observations are not only consistent with the pattern of the pseudocontact shifts of the heme protons, but also well account for the lower stability of V45H mutant against heat and urea.

PubMed: 15273310
DOI: 10.1110/ps.04721104

実験手法

SOLUTION NMR