Extended Data Fig. 5: Comparison of CryoEM map of MarDK to AlphaFold 3 models. | Nature Catalysis

Extended Data Fig. 5: Comparison of CryoEM map of MarDK to AlphaFold 3 models.

From: Architecture, catalysis and regulation of methylthio-alkane reductase for bacterial sulfur acquisition from volatile organic compounds

Extended Data Fig. 5

A) AlphaFold 3 predicted locations for MarD residues 1-65, 188-197, and 372-409 and MarK residues 1-26 and 88-93. MarK helix h7 (residues 86-93) and MarD residues 188-197 are predicted to reside under and adjacent to MarH when bound (as shown in panel A). Theses correspond to a lower ( < 3.5 Å) to no-resolution region in the Cryo-EM map in panel B. B) Local resolution plot of the final Cryo-EM map for MarDK from Extended Data Fig. 4 at a relatively lower threshold showing the lower- to no-resolution region at the MarD surface. C) Overlay of Cryo-EM electron density map (from B; in gray) and AlphaFold 3 model (from A).

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