Nature's optimization of protein functions is a highly intricate evolutionary process. In addition to optimal tertiary folding, the intramolecular recognition among the monomers that generates higher order quaternary arrangements is driven by stabilizing interactions that have a pivotal role for ideal activity. Homotetrameric avidin and streptavidin are regularly utilized in many applications, whereby their ultra-high affinity towards biotin is dependent on their quaternary arrangements. In recent years, a new subfamily of avidins was discovered that comprises homodimers rather than tetramers, in which the high affinity towards biotin is maintained. Intriguingly, several of the respective dimers have been shown to assemble into higher order cylindrical hexamers or octamers that dissociate into dimers upon biotin binding. Here, you can see the structure of wilavidin, a newly discovered member of the dimeric subfamily, forming hexamers in the apo form which are uniquely maintained upon biotin binding with six high affinity binding sites. The represented structure of wilavidin in complex with biotin, was determined by X-ray crystallography at a resolution of 1.6 Amgstrons (PDB code: 7P8Z)
#molecularart ... #immolecular ... #wilavidin ... #biotin ... #complex ... #streptavidin ... #xray
Protein rendered with @proteinimaging and composed by @corelphotopaint
#molecularart ... #immolecular ... #wilavidin ... #biotin ... #complex ... #streptavidin ... #xray
Protein rendered with @proteinimaging and composed by @corelphotopaint
