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. 2018 Dec 14;13(12):e0208850. doi: 10.1371/journal.pone.0208850

Fig 5. Close-up views of PLP-binding regions and structure-based alignements of SHMTs.

Fig 5

(A) Close-up view of the PLP-binding region of TtSHMT (left panel), EcSHMT (middle panel) and of a model of HpSHMT apoprotein with PLP (right panel). Contributions of chains A and B and the positions of loops 1, 2, 3, 4, 5, 6 and 7 are indicated in cyan, purple, red, pale green, grey, pink and wheat, respectively. The following residues are missing in loop 1 and 3: 54–67 (53–66) and 124–130 (120–134) from HpSHMT monomer A (monomer B). (B) Structure-based alignments of the protein sequences of SHMTs from E. coli, T. thermophilus and H. pylori highlighting structural elements, conserved features (dots), conserved loops 1–7 and residues acting on loop 3 conformation (stars). (C) Close-up of the “open lid” conformation of loop 3 from HpSHMT colored in red versus the “closed lid” conformation from EcSHMT colored in blue. Loop 5 is colored in blue and pale green for EcSHMT and HpSHMT, respectively.