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. 2020 Feb 2;295(11):3708–3718. doi: 10.1074/jbc.RA119.012256

Figure 4.

Figure 4.

Details of the soybean SHMT8 ligand complexes. A, the enzyme–PLP complex as an internal aldimine with Lys-244 (yellow). Chain A of Essex SHMT8 is in pink, and chain B is purple. The Forrest SHMT8 (white) complex with PLP (gray) is superimposed. Side chains of key residues involved in ligand interactions are shown as sticks. B, The SHMT8 complexes with PLP-Gly complex as an external aldimine (yellow). The colors as described for A. Hydrogen bonds to the glycine adduct are shown. C, the 1.4 Å resolution Essex SHMT8 ternary complex with PLP-Gly and FTHF. FTHF is cyan, and the other colors are as in A; two conformers of FTHF are shown (major with thicker lines) with different positions of the formyl oxygen. Side chains of residues involved in ligand interactions are shown as sticks. The two Forrest polymorphic residues are highlighted in green. D, the THF-binding loop in the Essex SHTM8·PLP-Gly·FTHF complex showing how it packs against FTHF in its closed conformation.