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Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G.
- Source :
-
Journal of Structural Biology . Jun2023, Vol. 215 Issue 2, pN.PAG-N.PAG. 1p. - Publication Year :
- 2023
-
Abstract
- [Display omitted] • A high-quality cryo-EM structure of malate synthase G (MSG) at 2.89 Å. • A complete structural comparison of a 723-residue MSG determined by cryo-EM and X-ray crystallography. • Cryo-EM revealed the structural dynamics of MSG. • The structural dynamics unraveled by cryo-EM, crystallography and NMR are highly correlated. 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10478477
- Volume :
- 215
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Journal of Structural Biology
- Publication Type :
- Academic Journal
- Accession number :
- 163796360
- Full Text :
- https://doi.org/10.1016/j.jsb.2023.107958