Science Advances

Supplementary Materials

This PDF file includes:

  • Table S1. Data collection and refinement statistics.
  • Table S2. Dissociation constants for binding of MMOH and MMOB, MMOD, and truncated MMOD proteins.
  • Table S3. Active-site Fe-Fe distances in MMOH structures.
  • Fig. S1. Primary sequence conservation of M. trichosporium OB3b and M. sporium strain 5 MMOHs and multiple sequence alignment of MMOD.
  • Fig. S2. Crystal structure of the M. capulatus MMOH-MMOB complex (PDB ID: 4GAM) and the structural comparison of MMOD (M. sporium strain 5) and MMOB (M. capsulatus) binding to MMOH.
  • Fig. S3. Conformational changes in MMOH upon MMOD and MMOB binding.
  • Fig. S4. Geometry of the di-iron active site in the MMOH-MMOD complex and its structural comparison with other known MMOH structures.
  • Fig. S5. Comparison of the substrate access routes in MMOH (PDB ID: 1MHY), MMOH-MMOB complex (PDB ID: 4GAM), and MMOH-MMOD complex.
  • Fig. S6. Comparison of the internal cavities within the MMOH protomer of MMOH-MMOD complex, MMOH, and MMOH-MMOB complex.
  • Fig. S7. MMOD does not associate with DNA as well as copper ions.
  • References (39, 40)

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