Solution NMR structures of oxidized and reduced Ehrlichia chaffeensis thioredoxin: NMR-invisible structure owing to backbone dynamics

Buchko, G.W.; Hewitt, S.N.; Van Voorhis, W.C.; Myler, P.J.

doi:10.1107/S2053230X1701799X

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Both faces of the surface representation of the structure closest to the average for oxidized Ec-Trx, illustrating the locations of residues with missing amide cross peaks in ¹H–¹⁵N HSQC spectra. Residues with assigned amide ¹H–¹⁵N HSQC cross peaks are colored magenta. Residues with missing amide cross peaks in both redox states are colored blue and those missing after reduction of the Cys32–Cys35 disulfide bond are colored cyan. The active-site cysteine residues are colored yellow. The representation on the left is in approximately the same orientation as shown in Figs. 1

and 4

, with the representation on the right a 180° rotation about the y axis.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 74| Part 1| January 2018| Pages 46-56

https://doi.org/10.1107/S2053230X1701799X

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