Download MendeleyCrystal structures of Escherichia coli glucokinase and insights into phosphate binding.
Andrews, J., Sakon, J., Fan, C.(2025) Acta Crystallogr F Struct Biol Commun 81: 332-337
- PubMed: 40632113
- DOI: https://doi.org/10.1107/S2053230X25005515
- Primary Citation of Related Structures:
9DUC, 9DVZ - PubMed Abstract:
Here, we report the crystal structure of Escherichia coli glucokinase (GLK), which has phosphate bound in the cleft between the α and β domains adjacent to the active site. A ternary complex consisting of GLK, glucose and phosphate is also reported in this work. Diffraction data were collected at 2.63 Å resolution for the phospate-bound form (R work /R free = 0.191/0.230) and at 2.54 Å resolution for the ternary complex (R work /R free = 0.202/0.258), both at 297 K. A B-factor analysis of the phosphate-bound GLK structure revealed consistently lower values for phosphate-interacting basic residues in the α4, α5 and α9 helices, while significant root-mean-square deviation (r.m.s.d.) spikes indicated flexibility in regions preceding β1 and within the loop between the β5 and β6 sheets of the α domain. In the ternary complex, phosphate is bound adjacent to glucose, and the B factors for the α4, α5 and α9 helices were further reduced, while r.m.s.d. spikes were observed at the end of the β10 sheet and within the α6 helix of the β-domain. This structural characterization suggests that phosphate could influence the activity of GLK by altering glucose binding and modulating interactions with a loop-interacting regulatory protein.
- Department of Chemistry and Biochemistry, University of Arkansas at Fayetteville, Fayetteville, AR 72701, USA.
Organizational Affiliation:
