6I2Z

Isolated globin domain of the Bordetella pertussis globin-coupled sensor

Summary for 6I2Z

• Entry DOI: 10.2210/pdb6i2z/pdb
• Related: 4UIQ
• Descriptor: Uncharacterized protein, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: heme-based sensor, oxygen affinity, c-di-gmp and enzyme specificity, biofilm formation., transferase
• Biological source: Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
• Total number of polymer chains: 2
• Total formula weight: 41164.03

Authors

Germani, F.,De Schutter, A.,Cuypers, B.,Berghmans, H.,Van Hauwaert, M.-L.,Bruno, S.,Mozzarelli, A.,Moens, L.,Van Doorslaer, S.,Bolognesi, M.,Pesce, A.,Dewilde, S. (deposition date: 2018-11-02, release date: 2019-10-16, Last modification date: 2024-11-13)

Primary citation

Germani, F.,Nardini, M.,De Schutter, A.,Cuypers, B.,Berghmans, H.,Van Hauwaert, M.L.,Bruno, S.,Mozzarelli, A.,Moens, L.,Van Doorslaer, S.,Bolognesi, M.,Pesce, A.,Dewilde, S.
Structural and Functional Characterization of the Globin-Coupled Sensors ofAzotobacter vinelandiiandBordetella pertussis.
Antioxid.Redox Signal., 32:378-395, 2020

PubMed Abstract: Structural and functional characterization of the globin-coupled sensors (GCSs) from (GReg) and (GReg). Ultraviolet/visible and resonance Raman spectroscopies confirm the presence in GReg and GReg of a globin domain capable of reversible gaseous ligand binding. In GReg, an influence of the transmitter domain on the heme proximal region of the globin domain can be seen, and ' is higher than for other GCSs. The O binding kinetics suggests the presence of an open and a closed conformation. As for GReg, the fully oxygenated GReg show a very high diguanylate cyclase activity. The carbon monoxide rebinding to GReg indicates that intra- and intermolecular interactions influence the ligand binding. The globin domains of both proteins (GReg globin domain and GRegGb with cysteines (Cys16, 45, 114, 154) mutated to serines [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 GCSs. However, GReg-Gb* shows also a second dimerization mode. This article extends our knowledge on the GCS proteins and contributes to a better understanding of the GCSs role in the formation of bacterial biofilms. GReg and GReg conform to the GCS family, share a similar overall structure, but they have different properties in terms of the ligand binding. In particular, GReg shows an open and a closed conformation that in the latter form will very tightly bind oxygen. GReg has only one closed conformation. In both proteins, it is the fully oxygenated GCS form that catalyzes the production of the second messenger.

PubMed: 31559835
DOI: 10.1089/ars.2018.7690

Experimental method

X-RAY DIFFRACTION (3.2 Å)