8ed4 | pdb_00008ed4

Structure of the complex between the arsenite oxidase and its native electron acceptor cytochrome c552 from Pseudorhizobium sp. str. NT-26

spinqualitylabelsall models 8ed4, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ed4 is a 12 chain structure with sequence from Pseudorhizobium banfieldiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: 4MO, F3S, FES, GOL, HEC, HEM, MGD, O, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6VAL8_9HYPH Publication Abstract from PubMed The arsenite oxidase (AioAB) from Pseudorhizobium banfieldiae sp. strain NT-26 catalyzes the oxidation of arsenite to arsenate and transfers electrons to its cognate electron acceptor cytochrome c(552) (cytc(552)). This activity underpins the ability of this organism to respire using arsenite present in contaminated environments. The crystal structure of the AioAB/cytc(552) electron transfer complex reveals two A(2)B(2)/(cytc(552))(2) assemblies per asymmetric unit. Three of the four cytc(552) molecules in the asymmetric unit dock to AioAB in a cleft at the interface between the AioA and AioB subunits, with an edge-to-edge distance of 7.5 A between the heme of cytc(552) and the [2Fe-2S] Rieske cluster in the AioB subunit. The interface between the AioAB and cytc(552) proteins features electrostatic and nonpolar interactions and is stabilized by two salt bridges. A modest number of hydrogen bonds, salt bridges and relatively small, buried surface areas between protein partners are typical features of transient electron transfer complexes. Interestingly, the fourth cytc(552) molecule is positioned differently between two AioAB heterodimers, with distances between its heme and the AioAB redox active cofactors that are outside the acceptable range for fast electron transfer. This unique cytc(552) molecule appears to be positioned to facilitate crystal packing rather than reflecting a functional complex. The structure of the complex between the arsenite oxidase from Pseudorhizobium banfieldiae sp. strain NT-26 and its native electron acceptor cytochrome c(552).,Poddar N, Santini JM, Maher MJ Acta Crystallogr D Struct Biol. 2023 Apr 1;79(Pt 4):345-352. doi: , 10.1107/S2059798323002103. Epub 2023 Mar 30. PMID:36995233 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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