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Title: Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin .
Author: Grandori R Carey J
Journal: Protein Sci . Citation: V : 3 ( 12 ) P : 2185-93 Year: 1994 Type: ARTICLE
Literature: oryza Field: abstract Doc ID: pub7756978 Accession (PMID): 7756978
Abstract: Strong sequence similarity has been reported among WrbA ( the Trp repressor-binding protein of Escherichia coli ) ; Ycp4 , a protein of unknown function from the budding yeast Saccharomyces cerevisiae ; P25 , the pap1-dependent protein of the fission yeast Schizosaccharomyces pombe ; and the translation product of a partial cDNA sequence from rice seedling root ( Oryza sativa , locus Ricr02421a ; here referred to as RicR ) . Further homology search with the profile method indicates that all the above sequences are related to the flavodoxin family and , in turn , allows detection of the recently proposed flavodoxin-like proteins from E coli , MioC and the hypothetical protein YihB . We discuss sequence conservation with reference to the known 3-dimensional structures of flavodoxins . Conserved sequence and hydrophobicity patterns , as well as residue-pair interaction potentials , strongly support the hypothesis that these proteins share the alpha/beta twisted open-sheet fold typical of flavodoxins , with an additional alpha/beta unit in the WrbA family . On the basis of the proposed structural homology , we discuss the details of the putative FMN-binding sites . Our analysis also suggests that the helix-turn-helix motif we identified previously in the C-terminal region of the WrbA family is unlikely to reflect a DNA-binding function of this new protein family .
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