2014
DOI: 10.1007/s00894-014-2400-8
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Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein

Abstract: WrbA is a novel multimeric flavodoxin-like protein of unknown function. A recent high-resolution X-ray crystal structure of E. coli WrbA holoprotein revealed a methionine sulfoxide residue with full occupancy in the FMN-binding site, a finding that was confirmed by mass spectrometry. In an effort to evaluate whether methionine sulfoxide may have a role in WrbA function, the present analyses were undertaken using molecular dynamics simulations in combination with further mass spectrometry of the protein. Methio… Show more

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“…Insertion loop 1 distinguishes WrbA from classic flavodoxins (15). WrbA is tetrameric in solution (30,32,39,40) and in crystal structures (31,33,36,38), which is distinct from classic flavodoxins, which are monomeric/dimeric (15,16,32,(41)(42)(43)(44). The WrbA tetramer presents four active sites, each with a bound flavin cofactor.…”
mentioning
confidence: 99%
“…Insertion loop 1 distinguishes WrbA from classic flavodoxins (15). WrbA is tetrameric in solution (30,32,39,40) and in crystal structures (31,33,36,38), which is distinct from classic flavodoxins, which are monomeric/dimeric (15,16,32,(41)(42)(43)(44). The WrbA tetramer presents four active sites, each with a bound flavin cofactor.…”
mentioning
confidence: 99%