2C41

X-ray structure of Dps from Thermosynechococcus elongatus

Summary for 2C41

• Entry DOI: 10.2210/pdb2c41/pdb
• Descriptor: DPS FAMILY DNA-BINDING STRESS RESPONSE PROTEIN, CHLORIDE ION, TETRAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: iron-binding/oxidation protein, dps (dna-binding proteins from starved cells), iron binding, thermostable protein, thermophilic cyanobacterium, dna- binding protein, stress protein, iron-binding-oxidation protein complex
• Biological source: THERMOSYNECHOCOCCUS ELONGATUS
• Total number of polymer chains: 12
• Total formula weight: 217184.82

Authors

Ilari, A.,Franceschini, S.,Ceci, P.,Chiancone, E. (deposition date: 2005-10-14, release date: 2006-10-11, Last modification date: 2023-12-13)

Primary citation

Franceschini, S.,Ceci, P.,Alaleona, F.,Chiancone, E.,Ilari, A.
Antioxidant Dps Protein from the Thermophilic Cyanobacterium Thermosynechococcus Elongatus.
FEBS J., 273:4913-, 2006

PubMed Abstract: DNA-binding proteins from starved cells (Dps proteins) protect bacteria primarily from oxidative damage. They are composed of 12 identical subunits assembled with 23-symmetry to form a compact cage-like structure known to be stable at temperatures > 70 degrees C and over a wide pH range. Thermosynechococcus elongatus Dps thermostability is increased dramatically relative to mesophilic Dps proteins. Hydrophobic interactions at the dimeric and trimeric interfaces called Dps-like are replaced by salt bridges and hydrogen bonds, a common strategy in thermophiles. Moreover, the buried surface area at the least-extended Dps-like interface is significantly increased. A peculiarity of T. elongatus Dps is the presence of a chloride ion coordinated with threefold symmetry-related arginine residues lining the opening of the Dps-like pore toward the internal cavity. T. elongatus Dps conserves the unusual intersubunit ferroxidase centre that allows the Dps protein family to oxidize Fe(II) with hydrogen peroxide, thereby inhibiting free radical production via Fenton chemistry. This catalytic property is of special importance in T. elongatus (which lacks the catalase gene) in the protection of DNA and photosystems I and II from hydrogen peroxide-mediated oxidative damage.

PubMed: 17018059
DOI: 10.1111/J.1742-4658.2006.05490.X

Experimental method

X-RAY DIFFRACTION (1.81 Å)