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Figure 3
Structural comparison of abMltA with MltA enzymes from different species. (a) Structural comparison of abMltA with other orthologs. Currently available structures of MltAs from N. gonorrhoeae (ngMltA; PDB entry 2g6g), B. pseudomallei (bpMltA; PDB entry 6qk4) and E. coli (ecMltA; PDB entry 2pi8 for the complex structure with a substrate analog and PDB entry 2pic for the apo structure) were superimposed with the structure of abMltA. (b–e) Pairwise structural superimposition of abMltA with ngMltA (b), bpLtgG (c), ecMltA (complex structure) (d) and ecMltA (apo structure) (e). (f) Structural comparison of both chains of abMltA with closed and open forms of ecMltA demonstrated by superimposition. (g) The structure of the extra domain of abMltA. The chain is colored blue to red from the N-terminus to the C-terminus. (h) Topological representation of the extra domain of abMltA. N-term and C-term indicate the N-terminus and C-terminus, respectively. (i) Structural and sequence comparison of the extra domain of abMltA with that of ngMltA by superimposition. The red dotted box indicates the additional residues and structure in ngMltA. Secondary structures are presented with cylinders for α-helices and arrows for β-sheets. Completely conserved residues are colored red.

IUCrJ
Volume 8| Part 6| November 2021| Pages 921-930
ISSN: 2052-2525
https://doi.org/10.1107/S2052252521008666