2D21

NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)

2D21 の概要

• エントリーDOI: 10.2210/pdb2d21/pdb
• 分子名称: Maltose-binding periplasmic protein (1 entity in total)
• 機能のキーワード: stereo-array isotope labelling, sail, sugar binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P0AEX9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40753.15

構造登録者

Kainosho, M.,Torizawa, T.,Iwashita, Y.,Terauchi, T.,Ono, A.M.,Guntert, P. (登録日: 2005-09-02, 公開日: 2006-03-07, 最終更新日: 2024-05-29)

主引用文献

Kainosho, M.,Torizawa, T.,Iwashita, Y.,Terauchi, T.,Mei Ono, A.,Guntert, P.
Optimal isotope labelling for NMR protein structure determinations.
Nature, 440:52-57, 2006

PubMed Abstract: Nuclear-magnetic-resonance spectroscopy can determine the three-dimensional structure of proteins in solution. However, its potential has been limited by the difficulty of interpreting NMR spectra in the presence of broadened and overlapping resonance lines and low signal-to-noise ratios. Here we present stereo-array isotope labelling (SAIL), a technique that can overcome many of these problems by applying a complete stereospecific and regiospecific pattern of stable isotopes that is optimal with regard to the quality and information content of the resulting NMR spectra. SAIL uses exclusively chemically and enzymatically synthesized amino acids for cell-free protein expression. We demonstrate for the 17-kDa protein calmodulin and the 41-kDa maltodextrin-binding protein that SAIL offers sharpened lines, spectral simplification without loss of information, and the ability to rapidly collect the structural restraints required to solve a high-quality solution structure for proteins twice as large as commonly solved by NMR. It thus makes a large class of proteins newly accessible to detailed solution structure determination.

PubMed: 16511487
DOI: 10.1038/nature04525

実験手法

SOLUTION NMR