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. 2015 Sep 23;6:958. doi: 10.3389/fmicb.2015.00958

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Copyright © 2015 Aziz, Khaw, Monk, Brunk, Lewis, Loh, Mishra, Nagle, Satyanarayana, Dhakshinamoorthy, Luche, Kitchen, Andrews, Palsson and Charusanti.

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) or licensor 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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Comparative structural analysis of (A) PrpC and (B) AldA. In the left panel of (A), the region with the highest overlapping structural similarity between PrpC and AldA is shown in green. The putative binding site with catalytic residues H274 and D325 are shown in blue. In the native reaction, 2-methyl citrate synthase, oxaloacetate reacts with a CoA-ester (e.g., propionyl-CoA) to form (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate. The NADH binding site is 15 Å away from the closest residue in the green overlapping region, and is therefore not considered a part of the overlap. Shown in the right panel of (A) is a magnification of the putative binding site. In the left panel of (B), the region with the highest overlapping structural similarity is again shown in green. The putative binding site (violet) shows where lactic acid binds to the protein. The putative binding orientation of lactic acid is taken from an alignment with PDB entry 3o8j.