7YQM

2.9-angstrom cryo-EM structure of Ecoli malate synthase G

Summary for 7YQM

• Entry DOI: 10.2210/pdb7yqm/pdb
• EMDB information: 34029
• Descriptor: Malate synthase G (1 entity in total)
• Functional Keywords: glyoxylate, malate, msg, citric acid cycel, malate synthase g, biosynthetic protein
• Biological source: Escherichia coli DH5[alpha]
• Total number of polymer chains: 1
• Total formula weight: 80581.34

Authors

Wu, K.-P.,Wu, Y.-M.,Lu, Y.-C. (deposition date: 2022-08-08, release date: 2023-03-29, Last modification date: 2025-07-02)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.89 Å)