Science Advances

Supplementary Materials

The PDF file includes:

  • Fig. S1. Purification and ATPase activity of wild-type A3B3, mutant A3B(L65Y)3, and DF complexes.
  • Fig. S2. Electron micrographs of negatively stained wild-type and mutant A3B3 complexes.
  • Fig. S3. Comparison of the crown structures of wild-type and mutant A3B3 complexes.
  • Fig. S4. Magnified views of the nucleotide binding sites of the bindable forms in eA3B(L65Y)3.
  • Fig. S5. Comparison of the nucleotide binding sites of wild-type and mutant complexes.
  • Table S1. Data collection and refinement statistics.
  • Table S2. RMSD values in superimpositions for each A1B1 unit of eA3B(L65Y)3 in the crystal structures of A3B3 and V1 complexes.
  • Table S3. Contact surface areas between A and B subunits in various A1B1 forms (Å2).
  • Table S4. Sum of contact surface areas at the central domain in A3B32).
  • Table S5. RMSD values in superimpositions for each A1B1 unit of bA3B(L65Y)3 in the crystal structures of A3B3 and V1 complexes.
  • Legends for movies S1 to S4

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Other Supplementary Material for this manuscript includes the following:

  • Movie S1 (.mov format). AFM scan movie of the C-terminal side of the wild-type and mutant A3B3.
  • Movie S2 (.mov format). Conformational changes at the β-barrel domain induced by the mutation.
  • Movie S3 (.mov format). Conformational changes at the C-terminal domain of eA3B3 induced by the mutation.
  • Movie S4 (.mov format). Conformational changes of eA3B(L65Y)3 induced by binding AMP-PNP molecules.

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