1BCT

THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION

1BCT の概要

• エントリーDOI: 10.2210/pdb1bct/pdb
• 分子名称: BACTERIORHODOPSIN (1 entity in total)
• 機能のキーワード: photoreceptor
• 由来する生物種: Halobacterium salinarum
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P02945
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7538.01

構造登録者

Nolde, D.E.,Barsukov, I.L.,Lomize, A.L.,Arseniev, A.S. (登録日: 1993-07-07, 公開日: 1994-04-30, 最終更新日: 2024-05-22)

主引用文献

Barsukov, I.L.,Nolde, D.E.,Lomize, A.L.,Arseniev, A.S.
Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution.
Eur.J.Biochem., 206:665-672, 1992

PubMed Abstract: 546 NOESY cross-peak volumes were measured in the two-dimensional NOESY spectrum of proteolytic fragment 163-231 of bacterioopsin in organic solution. These data and 42 detected hydrogen bonds were applied for determining the peptide spatial structure. The fold of the polypeptide chain was determined by local structure analysis, a distance geometry approach and systematic search for energetically allowed side-chain rotamers which are consistent with experimental NOESY cross-peak volumes. The effective rotational correlation time of 6 ns for the molecule was evaluated from optimization of the local structure to meet NOE data and from the dependence on mixing time of the NiH/Ci alpha H cross-peak volumes of the residues in alpha-helical conformation. The resulting structure has two well defined alpha-helical regions, 168-191 and 198-227, with root-mean-square deviation 44 pm and 69 pm, respectively, between the backbone atoms in 14 final energy refined conformations. The alpha-helices correspond to transmembrane segments F and G of bacteriorhodopsin. The segment F contains proline 186, which introduces a kink of about 25 degrees with a disruption of the hydrogen bond with the NH group of the following residue. The segments are connected by a flexible loop region 192-197. Torsion angles chi 1 are unequivocally defined for 62% of side chains in the alpha-helices but half of them differ from electron cryo-microscopy (ECM) model of bacteriorhodopsin, apparently because of the low resolution of ECM. Nevertheless, the F and G segments can be packed as in the ECM model and with side-chain conformations consistent with all NMR data in solution.

PubMed: 1606953
DOI: 10.1111/j.1432-1033.1992.tb16972.x

実験手法

SOLUTION NMR