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![[Figure 7]](qh5071fig7mag.jpg)
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Figure 7
The domain architecture of human GMP synthase (PDB entry 2vxo) is distinctly different from that of A. fumigatus GMP synthase. (a) The crystal structure of human GMP synthase features a GATase domain (orange), an ATP-PPase domain (maroon) and a D2 dimerization subdomain (purple), which are conserved between species; the D1 dimerization subdomain (green) is unique to human GMP synthase (Welin et al., 2013  ). (b) Superimposition of GMP synthase structures from A. fumigatus (GATase domain, yellow; ATP-PPase domain, magenta; D2 domain, cyan) and human (colour coding retained) depict the lack of a D1 dimerization subdomain in the fungal equivalent. Alignment of the XMP-binding site residues (c) and ATP-binding site residues (d) of the GMP synthase ATP-PPase domains from A. fumigatus and H. sapiens reveals key differences in composition. |
![[Figure 7]](qh5071fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
