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Figure 1
(a) Superposition of cartoon representations of the structures of oxidized (PDB entry 6ali, wheat) and reduced (PDB entry 6amr, purple) Ec-Trx closest to the average structure in the calculation ensembles. The 21-­residue N-terminal tag has been removed for clarity, with the side chains of the active-site cysteine residues, Cys32 and Cys35, colored yellow (oxidized) and magenta (reduced). (b) The primary structure of Ec-Trx with the STRIDE elements of secondary structure identified in the reduced (re) and oxidized (ox) states (α-helices, red; β-strands, blue). Residues lacking an assigned amide cross peak are identified by hollow letters.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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