6onp | pdb_00006onp

Crystal structure of periplasmic binding protein XoxJ from Methylobacterium extorquens AM1

spinqualitylabelsall models 6onp, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6onp is a 1 chain structure with sequence from Methylorubrum extorquens AM1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C5B122_METEA Publication Abstract from PubMed Lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have been recently shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems comprise two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function), about which little is known. Here, we biochemically and structurally characterize these proteins from the methyltroph, Methylobacterium extorquens AM1. In contrast to results obtained via an artificial assay system, assays of XoxFs metallated with LaIII, CeIII, and NdIII using their physiological electron acceptor, XoxG, display Ln-independent activities, but the Km for XoxG markedly increases from La to Nd. This result suggests that XoxG's redox properties are tuned specifically for lighter Lns in XoxF, an interpretation supported by the unusually low reduction potential of XoxG (+172 mV). The x-ray crystal structure of XoxG provides a structural basis for this reduction potential and insight into the XoxG-XoxF interaction. Finally, the x-ray crystal structure of XoxJ reveals a large hydrophobic cleft and suggests a role in activation of XoxF. These studies enrich our understanding of the underlying chemical principles that enable the activity of XoxF with multiple lanthanides in vitro and in vivo. Biochemical and structural characterization of XoxG and XoxJ and their roles in activity of the lanthanide-dependent methanol dehydrogenase, XoxF.,Featherston ER, Rose HR, McBride MJ, Taylor E, Boal AK, Cotruvo J Jr Chembiochem. 2019 Apr 24. doi: 10.1002/cbic.201900184. PMID:31017712 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methanol dehydrogenase

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