Drosophila melanogaster frataxin: protein crystal and predicted solution structure with identification of the iron-binding regions

Rodrigues, A.V.; Batelu, S.; Hinton, T.V.; Rotondo, J.; Thompson, L.; Brunzelle, J.S.; Stemmler, T.L.

doi:10.1107/S2059798322011639

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
Orientation of iron-impacted residues and electron-density mapping on the crystal structure of Dfh as determined by 2D ¹H/¹⁵N-HSQC NMR spectroscopy and modeled by PDB entry 7n9i. Left: orientation 1 showing the α-helical plane of the protein. Right: orientation 2 showing the β-sheet plane of the molecule. Residues perturbed upon iron addition with δ > 1.0 (colored green, labeled, ball-and-stick structure) include Ala26, Leu27, Glu36 and Asn37 on helix 1, Asp45 on strand 1, Val55 and Asn56 on strand 2 and Thr70 on strand 3. Residues that disappeared (have lines that are broadened beyond recognition) upon iron addition (colored red) include Cys28, Asp29 and Thr35 located on helix 1, Ala47 on strand 2 and Asp50 on the strand 1/2 loop. Electron-density mapping on helix 1 and strand 1 show the interaction of the iron-binding residues with iron (red spheres).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 79| Part 1| January 2023| Pages 22-30

https://doi.org/10.1107/S2059798322011639

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