The structure of the complex between the arsenite oxidase from Pseudorhizobium banfieldiae sp. strain NT-26 and its native electron acceptor cytochrome c552

Poddar, N.; Santini, J.M.; Maher, M.J.

doi:10.1107/S2059798323002103

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 2
The structure of the AioAB/cytc₅₅₂ electron transfer complex. (a) The AioAB/cytc₅₅₂ complex as observed for chains ABI, CDJ and EFK (AioA in blue, AioB in cyan and cytc₅₅₂ in salmon). (b) The interface between AioAB and cytc₅₅₂. Residues that participate in the two salt bridges are shown. (c) The structure of cytochrome cytc₅₅₂. The four helices are labeled and the heme cofactor is shown in salmon. The heme Fe atom is coordinated by His38 and Met103. The protoporphyrin ring is covalently attached to Cys34 and Cys37. (d) `Open-book' representation of the AioAB/cytc₅₅₂ complex (AioAB is in red and cytc₅₅₂ is in blue) indicating the `footprint' of interacting residues for each protein. (e) The same view as in (d) colored according to the electrostatic surfaces (positive charge in blue, negative charge in red and neutral in white).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 79| Part 4| April 2023| Pages 345-352

https://doi.org/10.1107/S2059798323002103

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