1Y8B

Solution NMR-Derived Global Fold of Malate Synthase G from E.coli

1Y8B の概要

• エントリーDOI: 10.2210/pdb1y8b/pdb
• 関連するPDBエントリー: 1D8C 1P7T
• 分子名称: Malate synthase G (1 entity in total)
• 機能のキーワード: nmr global fold, apo-malate synthase g, 82 kda enzyme, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P37330
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81636.52

構造登録者

Tugarinov, V.,Choy, W.-Y.,Orekhov, V.Y.,Kay, L.E. (登録日: 2004-12-10, 公開日: 2005-01-11, 最終更新日: 2024-05-22)

主引用文献

Tugarinov, V.,Choy, W.-Y.,Orekhov, V.Y.,Kay, L.E.
Solution NMR-derived global fold of a monomeric 82-kDa enzyme.
Proc.Natl.Acad.Sci.USA, 102:622-627, 2005

PubMed Abstract: The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of high-molecular-weight, single-polypeptide proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli, which has been extensively characterized by NMR in the past several years.

PubMed: 15637152
DOI: 10.1073/pnas.0407792102

実験手法

SOLUTION NMR