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.

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

Farci, D;ESPOSITO, FRANCESCA;TRAMONTANO, ENZO;PIANO, DARIO
2015-01-01

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.
2015
Deinococcus radiodurans; Hexagonally packed intermediate; S-layer; SlpA, DR_2577; Microbiology; Microbiology (medical); Bacteria
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/110772
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