2L0M

DsbB2 peptide structure in 100% TFE

2L0M の概要

• エントリーDOI: 10.2210/pdb2l0m/pdb
• 関連するPDBエントリー: 2K73 2ZUQ
• 分子名称: Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I (1 entity in total)
• 機能のキーワード: dsbb, membrane protein, organic solvent, folding
• 由来する生物種: Escherichia coli BW2952
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (By similarity): C4ZTM6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2832.49

構造登録者

Hwang, S.,Hilty, C. (登録日: 2010-07-08, 公開日: 2011-03-09, 最終更新日: 2024-05-01)

主引用文献

Hwang, S.,Hilty, C.
Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy.
Proteins, 79:1365-1375, 2011

PubMed Abstract: The two-stage model for membrane protein folding postulates that individual helices form first and are subsequently packed against each other. To probe the two-stage model, the structures of peptides representing individual transmembrane helices of the disulfide bond forming protein B have been studied in trifluoroethanol solution as well as in detergent micelles using nuclear magnetic resonance (NMR) and circular dichroism spectroscopy. In TFE solution, peptides showed well-defined α-helical structures. Peptide structures in TFE were compared to the structures of full-length protein obtained by X-ray crystallography and NMR. The extent of α-helical secondary structure coincided well, lending support for the two-stage model for membrane protein folding. However, the conformation of some amino acid side chains differs between the structures of peptide and full-length protein. In micellar solution, the peptides also adopted a helical structure, albeit of reduced definition. Using measurements of paramagnetic relaxation enhancement, peptides were confirmed to be embedded in micelles. These observations may indicate that in the native protein, tertiary interactions additionally stabilize the secondary structure of the individual transmembrane helices.

PubMed: 21337621
DOI: 10.1002/prot.22877

実験手法

SOLUTION NMR