1FDM

FD MAJOR COAT PROTEIN IN SDS MICELLES, NMR, 20 STRUCTURES

1FDM の概要

• エントリーDOI: 10.2210/pdb1fdm/pdb
• 分子名称: FD MAJOR COAT PROTEIN (1 entity in total)
• 機能のキーワード: fd coat protein, membrane protein, micelles, coat protein, viral protein
• 由来する生物種: Enterobacteria phage fd
• 細胞内の位置: Virion (Potential): P69539
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5244.00

構造登録者

Almeida, F.C.L.,Opella, S.J. (登録日: 1997-05-28, 公開日: 1997-09-17, 最終更新日: 2024-05-22)

主引用文献

Almeida, F.C.,Opella, S.J.
fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix.
J.Mol.Biol., 270:481-495, 1997

PubMed Abstract: By performing multidimensional solution NMR experiments on micelle samples it was possible to determine the structure of the membrane-bound form of fd coat protein based on short-range distance and dihedral angle constraints using distance geometry and simulated annealing calculations. Its dynamics were described by 15N relaxation measurements (T1, T2, heteronuclear nuclear Overhauser enhancement (NOE)) fitted with the Lipari-Szabo model-free formalism adapted for the transmembrane and in-plane helices of a membrane protein. The overall correlation time of the protein in micelles was found to be approximately 9 ns, and the local motion of each backbone N-H vector was described by an order parameter and an effective correlation time. The 50 residue protein has an amphipathic alpha-helix (residues 7 to 16) and a hydrophobic alpha-helix (residues 27 to 44), which were found to be approximately perpendicular on the basis of NOEs in the residues that connect the two helices. The residues connecting the helices are of particular interest in membrane proteins, and in this case the loop consists of two turns. The relaxation data show the presence of an extra motion in the amphipathic alpha-helix on the nanosecond timescale and additional flexibility of several residues in the loop connecting the two helices.

PubMed: 9237913
DOI: 10.1006/jmbi.1997.1114

実験手法

SOLUTION NMR