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

ABSTRACT: 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. The structural implications of these findings are discussed providing new elements for a more integrated model of this S-layer.

SUBMITTER: Farci D

PROVIDER: S-EPMC4419837 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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

Farci Domenica D Bowler Matthew W MW Esposito Francesca F McSweeney Sean S Tramontano Enzo E Piano Dario D

Frontiers in microbiology 20150603

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. The structural implications ...[more]

PMID: 26074883

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