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. 2019 Jan 24;7:7. doi: 10.3389/fbioe.2019.00007

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Copyright © 2019 Isupov, Boyko, Sutter, James, Sayer, Schmidt, Schönheit, Nikolaeva, Stekhanova, Mardanov, Ravin, Bezsudnova, Popov and Littlechild.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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An overlay of the Cα trace of the AF0933 BCAT (green and coral coil) gabaculine complex with the Nectria TAm (ice blue and gold coil) gabaculine complex (Sayer et al., 2014) to illustrate the differences between the ligand and loop conformations within the active site between the two enzymes. The PLP gabaculine adduct is shown as a stick model for the AF0933 BCAT structure and as thick lines for the Nectria amine TAm structure. Interdomain loops and the loop connecting β5 and β6 of the N-terminal small domain of the adjacent subunit in the catalytic dimer covering the active site cavity, have different conformation between the AF0933 BCAT and the Nectria TAm as shown.