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. 2017 Mar 13;4:12. doi: 10.3389/fmolb.2017.00012

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Copyright © 2017 Prischi and Pastore.

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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Ribbon representation of CyaY and IscS-IscU interactions. (A) IscU is shown in pink, while IscS monomers are colored in pale cyan and light green with side chains of residues mutated indicated explicitly: R220E/R223E/R225E (red). PLP in IscS active site is shown in black. Side chains of CyaY residues exhibiting CSP are explicitly shown: residues interacting with IscS are in red (Trp14, Leu15, Glu19, Asp22, Asp23, Trp24, Asp25, Asp27, Ser28, Asp29, Ile30, Asp31, Cys32, Glu33, Ile34, Leu39, Thr42, Phe43, Glu44, and Gly46), while residues interacting with IscU are in green (Thr40, Ile41, Lys48, Ile50, Asp52, Arg53, Glu55, Trp61, Leu62, Ala63, Thr64, Gln66, Gly68, Tyr69, and His70). (B) Electrostatic surface of unbound Iscs. The circle indicates the position of the positively charged residues involved in binding.