3D domain swapping in the TIM barrel of the α subunit of Streptococcus pneumoniae tryptophan synthase

Michalska, K.; Kowiel, M.; Bigelow, L.; Endres, M.; Gilski, M.; Jaskolski, M.; Joachimiak, A.

doi:10.1107/S2059798320000212

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
The SpTrpA 3D domain-swapped dimer. (a) The 3D domain swapping of protein chains C (yellow) and D (green). (b) Topology of the secondary-structure elements viewed down the axis of the 3D domain-swapped TIM barrel of SpTrpA. Helices are marked as circles and labeled H0–H8; β-strands are marked as triangles and labeled S1–S8. Residue ranges for the α-helices and β-strands are marked in Supplementary Fig. S1. (c) The domain-swapping hinge (residues Ile55–Gly64) of chain C (yellow) and chain D (green), shown as 2F_o − F_c electron density contoured at 1.2σ.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 76| Part 2| February 2020| Pages 166-175

https://doi.org/10.1107/S2059798320000212

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