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. 2022 Mar 11;78(Pt 4):494–508. doi: 10.1107/S2059798322001772

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© Onisha Patel et al. 2022

This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

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Structural homology and surface representation of the enclosed cavities in MSMEG_0317Δ. (a) Comparison of the MSMEG_0317Δ fold with the CD36 superfamily of scavenger receptor proteins, including the human lysosomal integral membrane protein 2 (LIMP-2) and CD36, a fatty-acid transporter, which show an extended asymmetric β-barrel core. (b) Comparison of the MSMEG_0317Δ enclosed cavities with the CD36 cavity which binds palmitic acid. (c) Close-up of MSMEG_0317Δ cavity 1 entrance 1. (d) Close-up of MSMEG_0317Δ cavity 1 entrance 2. (e) Close-up of MSMEG_0317Δ cavity 2. Hydrogen-bond and salt-bridge interactions are shown as black dashed lines. See also Supplementary Fig. S5.