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Publication Abstract from PubMed

AIMS: Structural and functional characterization of the globin coupled sensors (GCS) of <i>Azotobacter vinelandii </i>(AvGReg) and <i>Bordetella pertussis</i> (BpeGReg). RESULTS: UV/Vis and RR spectroscopies confirm the presence in <i>Av</i>GReg and <i>Bpe</i>GReg of a globin domain capable of reversible gaseous ligand binding. In <i>Av</i>GReg an influence of the transmitter domain on the heme proximal region of the globin domain can be seen, and <i>k'</i>CO is higher than for other GCSs. The O₂ binding kinetics suggest the presence of an open and a closed conformation. As for <i>Bpe</i>GReg, the fully oxygenated <i>Av</i>GReg show a very high DGC activity. The CO rebinding to <i>Bpe</i>GReg indicates that intra- and intermolecular interactions influence the ligand binding. The globin domains of both proteins (<i>Av</i>GReg-Gb and <i>Bpe</i>Greg-Gb*) share the same GCS fold, a similar proximal but a different distal side structure. They homodimerize through a G-H helical bundle as in other GCS. However, <i>Bpe</i>GReg-Gb* shows also a second dimerization mode. INNOVATION: This paper extends our knowledge on the GCS proteins and contributes to a better understanding of the GCSs' role in the formation of bacterial biofilms. CONCLUSIONS: <i>Av</i>GReg and <i>Bpe</i>Greg conform to the GCS family, share a similar overall structure but they have different properties in terms of the ligand binding. In particular, <i>Av</i>Greg shows an open and closed conformation that in the latter form will very tightly bind oxygen. <i>Bpe</i>GReg has only one closed conformation. In both proteins, it is the fully oxygenated GCS form that catalyzes the production of the second messenger.

Structural and functional characterization of the globin-coupled sensors of <i>Azotobacter vinelandii </i>and <i>Bordetella pertussis</i>.,Germani F, Nardini M, De Schutter A, Cuypers B, Berghmans H, Van Hauwaert ML, Stefano B, Mozzarelli A, Moens L, Van Doorslaer S, Bolognesi M, Pesce A, Dewilde S Antioxid Redox Signal. 2019 Sep 27. doi: 10.1089/ars.2018.7690. PMID:31559835^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.