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. 2015 Dec 2;5:15493. doi: 10.1038/srep15493

Figure 1. Overall structure of ATP-bound MsFadD32.

Figure 1

(A) Ribbon representation of the MsFadD32 structure. The three subdomains of the N-terminal domain are colored green, wheat, and cyan, respectively. The insertion motif and C-terminal domain are colored orange and magenta, respectively. ATP is shown as yellow sticks. (B) The interactions between the insertion motif and N-terminal subdomain C. (C) The interactions between the insertion motif and C-terminal domain. (D) The ATP-bound MsFadD32 adopts an atypical adenylate-forming conformation. In (C–D), the residues involved are shown as sticks and the hydrogen bonds are shown as dashed lines.