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Figure 4
FnNanK lacks the cysteine-rich zinc-binding motif. (a) Structural comparison of apo FnNanK in red and substrate-bound (ManNAc, ADP and Mg2+) hMNK in green. (b) Superimposition of the substrate-binding regions of bacterial NanKs. The putative residues involved in catalysis in the substrate-binding site in FnNanK (blue) are superimposable with the corresponding residues in NanK from E. coli (EcNanK; PDB entry 2aa4, pink) and L. monocytogenes (LmNanK; PDB entry 4htl, green). The zinc-binding motif is only visible in EcNanK, which is represented by the coordination of Cys173, Cys166, Cys168 and His156 to the Zn atom (grey). The highly conserved histidine that coordinates ManNAc is present in FnNanK and EcNanK but corresponds to a tyrosine in LmNanK.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 73| Part 6| June 2017| Pages 356-362
https://doi.org/10.1107/S2053230X17007439
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