7YQN

Crystal structure of Ecoli malate synthase G

7YQN の概要

• エントリーDOI: 10.2210/pdb7yqn/pdb
• 関連するPDBエントリー: 7YQM
• EMDBエントリー: 34029 34030
• 分子名称: Malate synthase G, CHLORIDE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: glyoxylate, malate, msg, citric acid cycel, malate synthase g, biosynthetic protein
• 由来する生物種: Escherichia coli DH5[alpha]
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 161839.67

構造登録者

Wu, K.-P.,Lu, Y.-C.,Ko, T.-P. (登録日: 2022-08-08, 公開日: 2023-03-29, 最終更新日: 2023-11-29)

主引用文献

Ho, M.R.,Wu, Y.M.,Lu, Y.C.,Ko, T.P.,Wu, K.P.
Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G.
J.Struct.Biol., 215:107958-107958, 2023

PubMed Abstract: Determination of sub-100 kDa (kDa) structures by cryo-electron microscopy (EM) is a longstanding but not straightforward goal. Here, we present a 2.9-Å cryo-EM structure of a 723-amino acid apo-form malate synthase G (MSG) from Escherichia coli. The cryo-EM structure of the 82-kDa MSG exhibits the same global folding as structures resolved by crystallography and nuclear magnetic resonance (NMR) spectroscopy, and the crystal and cryo-EM structures are indistinguishable. Analyses of MSG dynamics reveal consistent conformational flexibilities among the three experimental approaches, most notably that the α/β domain exhibits structural heterogeneity. We observed that sidechains of F453, L454, M629, and E630 residues involved in hosting the cofactor acetyl-CoA and substrate rotate differently between the cryo-EM apo-form and complex crystal structures. Our work demonstrates that the cryo-EM technique can be used to determine structures and conformational heterogeneity of sub-100 kDa biomolecules to a quality as high as that obtained from X-ray crystallography and NMR spectroscopy.

PubMed: 36997036
DOI: 10.1016/j.jsb.2023.107958

実験手法

X-RAY DIFFRACTION (1.6 Å)