Structural basis of the dominant inheritance of hypermethioninemia associated with the Arg264His mutation in the MAT1A gene

Panmanee, J.; Antonyuk, S.V.; Hasnain, S.S.

doi:10.1107/S2059798320006002

Figure 3
Structural comparison of the apo form of wild-type MATα1 and the R264H mutant. Wild-type MATα1 and the MATα1 R264H mutant are shown as pink and blue ribbons, respectively, with alignment of chain A of each protein. (a) The dimer interface is represented by dashed lines; the C^α–C^α distances between the Arg264 or His264 residues of each protein are illustrated. C^α atoms are marked by yellow circles. (b) The distance displacements caused by the R264H mutation are shown by C^α–C^α measurements (blue dots) of these residues (Val262–Ile267) in each subunit compared with the wild type. The Thr262–Ile266 main chains are shown as dark pink (wild type) and blue (R264H mutant) sticks. C^α atoms are marked by yellow circles. (c) The dimer–dimer interface of wild-type MATα1 is shown in red (chains C and D). The areas in the dashed and solid boxes are enlarged in (d) and (e), respectively. (d) The polar interactions at the dimer–dimer interface found in the wild type are illustrated for chain A with chain C and for chain B with chain D. The residues of chains A and B are shown as pink sticks (pink labels), while the residues of chains C and D are shown as red sticks (red labels). (e) The distance displacements of Thr62 and Arg84 caused by the R264H mutation are shown compared with the wild type. Thr62 and Arg84 are presented as pink and red sticks for the wild type and as blue sticks for the R264H mutant. The Thr262–Ile266 main chains are shown as dark pink (wild type) and blue (R264H mutant) sticks to mark the mutation regions.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 76| Part 6| June 2020| Pages 594-607

https://doi.org/10.1107/S2059798320006002

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