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Fig. 3 | Biology Direct

Fig. 3

From: Structural modelling of the lumenal domain of human GPAA1, the metallo-peptide synthetase subunit of the transamidase complex, reveals zinc-binding mode and two flaps surrounding the active site

Fig. 3

Comparison of zinc ion binding regions in M28-type metallo-proteases and in human GPAA1 model structures. a We present the canonical Zn-binding sites (in sticks) of a few one zinc-bound cyclotransferase proteins (4fwu, 4mhn, 4yu9, 3pbe; top left) and of a few two zinc-bound aminopeptidase/carboxypeptidase proteins (1amp, 1rtq, 2anp, 2c6g; top right). The labels and numbering are shown in accordance with the reference structures 4fwu (magenta; T98 and L187) and 1amp (orange, D116 and M180), respectively. The interactions between residues T98 and L187 (in lines) adjacent to site 2 and site 4 in the one zinc-bound cyclotransferase are represented as dashes. The five canonical active site residues of the GPAA1Zn model (bottom left) are shown in green together with the nearby residues T155 and L227. b The distribution of the corresponding distances between the two residues during molecular dynamics trajectories are shown in magenta (T98 and L187 for 4fwu), black (T155 and L227 for GPAA1Zn), and in gray (T155 and L227 for GPAA1Zn1Zn2)

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Biology Direct

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