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Title: Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans

The protein DR_2577 is a major Surface layer component of the radio-resistant bacterium Deinococcus radiodurans. In the present study DR_2577 has been purified and its oligomeric profile characterized by means of size exclusion chromatography and gel electrophoresis. DR_2577 was found to be organized into three hierarchical orders characterized by monomers, stable dimers formed by the occurrence of disulfide bonds, and hexamers resulting from a combination of dimers. Finally, the structural implications of these findings are discussed providing new elements for a more integrated model of this S-layer.
 [1] ;  [2] ;  [1] ;  [3] ;  [1] ;  [4]
  1. Univ. of Cagliari, Cagliari (Italy)
  2. European Molecular Biology Lab. (EMBL), Grenoble (France); Univ. Grenoble, Grenoble (France). Alpes-EMBL-National Center for Scientific Research
  3. Brookhaven National Lab. (BNL), Upton, NY (United States). Dept. of Photon Sciences
  4. Univ. of Cagliari, Cagliari (Italy); International Institute of Molecular and Cell Biology, Warsaw (Poland)
Publication Date:
OSTI Identifier:
Report Number(s):
Journal ID: ISSN 1664-302X
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Frontiers in Microbiology
Additional Journal Information:
Journal Volume: 6; Journal ID: ISSN 1664-302X
Frontiers Research Foundation
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; S-layer; hexagonally packed intermediate; SlpA; DR_2577; Deinococcus radiodurans