2KWD

Supramolecular Protein Structure Determination by Site-Specific Long-Range Intermolecular Solid State NMR Spectroscopy

2KWD の概要

• エントリーDOI: 10.2210/pdb2kwd/pdb
• 関連するPDBエントリー: 2KQ4
• 分子名称: Immunoglobulin G-binding protein G (1 entity in total)
• 機能のキーワード: gb1, crystal packing, solid-state, quaternary structure, tedor, immune system
• 由来する生物種: Streptococcus sp. 'group G'
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): P19909
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 31144.05

構造登録者

Nieuwkoop, A.J.,Rienstra, C.M. (登録日: 2010-04-05, 公開日: 2010-06-02, 最終更新日: 2024-05-01)

主引用文献

Nieuwkoop, A.J.,Rienstra, C.M.
Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy.
J.Am.Chem.Soc., 132:7570-7571, 2010

PubMed Abstract: We demonstrate that 3D Z-filtered TEDOR experiments, when performed on mixtures of isotopically labeled protein samples, report on site-specific intermolecular distance restraints. These data sets can be leveraged to perform rigorous structure calculations of the protein interface. In the example demonstrated here, we determine the packing arrangement of our nanocrystalline GB1 preparation to be consistent with the trigonal form as determined by X-ray diffraction. This represents an important proof of principle, in a case where the results can be directly compared with other structural information. We envision the application of this approach to determining the registry and quaternary arrangement of protein fibrils, which most often cannot be determined by diffraction methods.

PubMed: 20465251
DOI: 10.1021/ja100992y

実験手法

SOLID-STATE NMR