6esv

Structure of the phosphate-bound form of AioX from Rhizobium sp. str. NT-26

spinqualitylabelsall models 6esv, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6esv is a 1 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 1.78Å Ligands: MSE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L0NML6_9HYPH Publication Abstract from PubMed Arsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that's role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate. A new family of periplasmic-binding proteins that sense arsenic oxyanions.,Badilla C, Osborne TH, Cole A, Watson C, Djordjevic S, Santini JM Sci Rep. 2018 Apr 19;8(1):6282. doi: 10.1038/s41598-018-24591-w. PMID:29674678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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