Bradavidin II from Bradyrhizobium japonicum: A new avidin-like biotin-binding protein

Structural Adaptation of a Thermostable Biotin-binding Protein in a Psychrophilic Environment

“…A distinctive feature in shwanavidin, thus far observed only in the structure of rhizavidin, is a disulfide bridge between Cys-45 and Cys-74 linking the L3,4 and L5,6 loops, respectively. Additionally, conserved Cys residues were also found in homologous positions in sequences of other proteobacteria avidin-like proteins, whose structural characteristics have yet to be studied (5,7,8).…”

“…Historically, the first avidin to be documented was from the egg white of chicken and other avian species (1). Later, streptavidins from a few Streptomyces species (4), and, more recently, isolated examples of avidin-like proteins were discovered in other prokaryotic (5)(6)(7)(8) and eukaryotic (fungal) sources (9). Despite the sporadic but wide distribution of high affinity biotin-binding avidinlike proteins, their precise function in nature is essentially unknown.…”

Crystal Structure of Rhizavidin: Insights into the Enigmatic High-Affinity Interaction of an Innate Biotin-Binding Protein Dimer

“…This feature is not unique to rhizavidin, since the recently characterized avidin-like proteins, bradavidin and bradavidin II, appear to contain a disulfide in an identical position although their three-dimensional structures are currently unavailable. 30 The polar interactions between biotin and rhizavidin are highly similar to those of the other avidins. The biotin bicyclic ring system forms an identical Hbonding network in all proteins (Fig.…”

Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail

“…Novel proteins were discovered, among them avidin-related proteins (AVRs) (Laitinen et al, 2002) and bradavidin (Helppolainen et al, 2008;Leppiniemi et al, 2012;Nordlund et al, 2005), all exhibiting a tetrameric assembly. More recent studies, however, have revealed additional biotin-binding proteins, which display dimeric rather than tetrameric arrangements, while maintaining their high-affinity binding of biotin (Helppolainen et al, 2007;Meir et al, 2012Meir et al, , 2009.…”