6ONP

Crystal structure of periplasmic binding protein XoxJ from Methylobacterium extorquens AM1

Summary for 6ONP

• Entry DOI: 10.2210/pdb6onp/pdb
• Descriptor: periplasmic binding protein XoxJ, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: perisplasmic binding protein, solute-binding protein, methanol dehydrogenase, unknown function
• Biological source: Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
• Total number of polymer chains: 1
• Total formula weight: 31251.85

Authors

Rose, H.R.,Taylor, E.M.,Boal, A.K. (deposition date: 2019-04-22, release date: 2019-05-08, Last modification date: 2024-10-23)

Primary citation

Featherston, E.R.,Rose, H.R.,McBride, M.J.,Taylor, E.M.,Boal, A.K.,Cotruvo Jr., J.A.
Biochemical and Structural Characterization of XoxG and XoxJ and Their Roles in Lanthanide-Dependent Methanol Dehydrogenase Activity.
Chembiochem, 20:2360-2372, 2019

PubMed Abstract: Lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have recently been shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems contain two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function), about which little is known. In this work, we have biochemically and structurally characterized these proteins from the methyltroph Methylobacterium extorquens AM1. In contrast to results obtained in an artificial assay system, assays of XoxFs metallated with La , Ce , and Nd using their physiological electron acceptor, XoxG, display Ln-independent activities, but the K 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 the 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.

PubMed: 31017712
DOI: 10.1002/cbic.201900184

Experimental method

X-RAY DIFFRACTION (2.27 Å)