Life Sciences and cultural heritage Figure 1. (a) Msd dimer with the core CDA-fold. Unique elements, including the α4-α5 loop, are highlighted in yellow; (b) MD simulation captures the enzyme in various conformations. Distance between side-chain of residues from the β2-α2 loop and from the α4-α5 loop shows the population of different conformations in apo and analog bound state; (c) Snapshots of different conformations of the enzyme depicting the gating motion. The β2-α2 loop is in green and the α4-α5 loop is in yellow; (d) Experimental validation of the role of gating loops in deamination. Residues from the gating loops are highlighted; Structural analysis of α4-α5 loop shows the position of the di-proline motif (e) in P122A and (f) ΔP123 as compared to native (in yellow); (g) The distribution profile of RMSD of the α4-α5 loop; (h) B-factor occupancy plot of native Msd and P122A. The colouring spectrum depicts blue as the regions with lowest B-factor and red as the highest B-factor; (i) Snapshot of closed states in native and P122A highlighting the importance of P122_W95* stacking in facilitating closure. (All the figures are adapted from S. Porathoor et al., Nucleic Acids Research. 2025 licensed under CC BY NC). S. Porathoor1, A. R. Choudhury1, R. Chakrabarti1, R. Anand1 1 Department of Chemistry, Indian Institute of Technology Bombay, Mumbai, India e-mail: ruchi@chem.iitb.ac.in Acknowledgments The research leading to this result has been supported by the Department of Biotechnology, Ministry of Science & Technology, Government of India [BT/HRD/NWBA/39/03/2018- 19]; and Science and Engineering Research Board [CRG/ 2020/000279]. Original paper S. Porathoor et al., Nucleic Acids Research. 53, 6, (2025); DOI:10.1093/nar/gkaf171. Fig. 1 (a) (g) (d) (b) (c) (e) (f) (h) (i) Elettra Highlights 2024–2025 71
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