6x9g | pdb_00006x9g

Structure of the malonate-bound form of ArrX from Chrysiogenes arsenatis

spinqualitylabelsall models 6x9g, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6x9g is a 1 chain structure with sequence from Chrysiogenes arsenatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.68Å Ligands: MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The anaerobic bacterium Chrysiogenes arsenatis respires using the oxyanion arsenate (AsO4(3-)) as the terminal electron acceptor, where it is reduced to arsenite (AsO3(3-)) while concomitantly oxidizing various organic (e.g., acetate) electron donors. This respiratory activity is catalyzed in the periplasm of the bacterium by the enzyme arsenate reductase (Arr), with expression of the enzyme controlled by a sensor histidine kinase (ArrS) and a periplasmic-binding protein (PBP), ArrX. Here, we report for the first time, the molecular structure of ArrX in the absence and presence of bound ligand arsenate. Comparison of the ligand-bound structure of ArrX with other PBPs shows a high level of conservation of critical residues for ligand binding by these proteins; however, this suite of PBPs shows different structural alterations upon ligand binding. For ArrX and its homologue AioX (from Rhizobium sp. str. NT-26), which specifically binds arsenite, the structures of the substrate-binding sites in the vicinity of a conserved and critical cysteine residue contribute to the discrimination of binding for these chemically similar ligands. Structural and Functional Investigation of the Periplasmic Arsenate-Binding Protein ArrX from Chrysiogenes arsenatis.,Poddar N, Badilla C, Maghool S, Osborne TH, Santini JM, Maher MJ Biochemistry. 2021 Feb 16;60(6):465-476. doi: 10.1021/acs.biochem.0c00555. Epub, 2021 Feb 4. PMID:33538578 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA