4H5B

Crystal Structure of DR_1245 from Deinococcus radiodurans

Summary for 4H5B

• Entry DOI: 10.2210/pdb4h5b/pdb
• Descriptor: DR_1245 protein, BROMIDE ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: secretion chaperone-like fold, unknown function
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 2
• Total formula weight: 35820.84

Authors

Norais, C.,Servant, P.,Bouthier-de-la-Tour, C.,Coureux, P.D.,Ithurbide, S.,Vannier, F.,Guerin, P.,Dulberger, C.L.,Satyshur, K.A.,Keck, J.L.,Armengaud, J.,Cox, M.M.,Sommer, S. (deposition date: 2012-09-18, release date: 2013-01-30, Last modification date: 2024-02-28)

Primary citation

Norais, C.,Servant, P.,Bouthier-de-la-Tour, C.,Coureux, P.D.,Ithurbide, S.,Vannier, F.,Guerin, P.P.,Dulberger, C.L.,Satyshur, K.A.,Keck, J.L.,Armengaud, J.,Cox, M.M.,Sommer, S.
The Deinococcus radiodurans DR1245 Protein, a DdrB Partner Homologous to YbjN Proteins and Reminiscent of Type III Secretion System Chaperones.
Plos One, 8:e56558-e56558, 2013

PubMed Abstract: The bacterium Deinococcus radiodurans exhibits an extreme resistance to ionizing radiation. A small subset of Deinococcus genus-specific genes were shown to be up-regulated upon exposure to ionizing radiation and to play a role in genome reconstitution. These genes include an SSB-like protein called DdrB. Here, we identified a novel protein encoded by the dr1245 gene as an interacting partner of DdrB. A strain devoid of the DR1245 protein is impaired in growth, exhibiting a generation time approximately threefold that of the wild type strain while radioresistance is not affected. We determined the three-dimensional structure of DR1245, revealing a relationship with type III secretion system chaperones and YbjN family proteins. Thus, DR1245 may display some chaperone activity towards DdrB and possibly other substrates.

PubMed: 23441204
DOI: 10.1371/journal.pone.0056558

Experimental method

X-RAY DIFFRACTION (2 Å)