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Fig. 8 | BMC Plant Biology

Fig. 8

From: Determinants of substrate specificity in a catalytically diverse family of acyl-ACP thioesterases from plants

Fig. 8

Residues within regions that influence ALT substrate specificity may contribute to interactions with ACPs. A Ribbon model of the maximum likelihood docking confirmation of E. coli acyl carrier protein (yellow, PDB ID 2FAC) with the AtALT4 homotetramer (grey) [51]. The predicted active site residue of AtALT4, Asp17, is located at 13.5 Å from of S36 on ACP, which is necessary to accommodate rotation of the tethered acyl chain carrier by ACP about the phosphopantethiene arm [33, 34]. Docking of AtALT4 with E. coli ACPs was performed using the ClusPro server, and docking conformations were visualized in ChimeraX 1.2.5 software [42, 49, 50]. B Molecular surface model of the predicted ACP docking site of AtALT4. Residues within aa78–93 (blue), aa64–67 (green), and aa108–111 (purple) of the ALT thioesterase domain that form part of the interaction interface with docked ACP (yellow) are coloured and shown as stick models. Magnified views show inter-chain hydrogen bonds, represented as blue dashed lines, between residues of AtALT4 and of docked E. coli ACP

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