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. 2026 Jun 26;65(14):2227–2249. doi: 10.1021/acs.biochem.6c00318

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X-ray crystal structure of PFL-AE. (A) The overall structure of PFL-AE from E. coli shows an RS enzyme fold with a [4Fe-4S] cluster, AdoMet, and the 7-mer peptide bound (PDB ID: 3CB8). The 7-mer peptide is shown in red. (B) The [4Fe-4S] cluster is coordinated by C29, C33, and C36. (C) AdoMet coordinates the [4Fe-4S] cluster via its amino and carboxylate moieties, indicated by black arrows. The 5′C–SγMet bond which is homolytically cleaved is indicated with an arrow and labeled. (D) A 7-mer peptide mimicking the glycine loop of PFL (red) is bound in the active site of PFL-AE, with a Gly–Cα to AdoMet–C5′ distance consistent with other RS enzymes. All Fe atoms are shown in orange. All S atoms are shown in yellow.