|PROSITE documentation PDOC00499|
Avidin  is a minor constituent of egg white in several groups of oviparous vertebrates. Avidin, which was discovered in the 1920's, takes its name from the avidity with which it binds biotin. These two molecules bind so strongly that is highly difficult to separate them. Streptavidin is a protein produced by Streptomyces avidinii which also binds biotin and whose sequence is evolutionary related to that of avidin.
Avidin and streptavidin both form homotetrameric complexes of noncovalently associated chains. Each chain forms a very strong and specific non-covalent complex with one molecule of biotin.
Fibropellins I and III  are proteins that form the apical lamina of the sea urchin embryo, a component of the extracellular matrix. These two proteins have a modular structure composed of a CUB domain (see <PDOC00908>), followed by a variable number of EGF repeats (see <PDOC00021>) and a C-terminal avidin-like domain. The fibropellin avidin-like domain forms a homotetramer incapable of binding biotin .
The three-dimensional structures of both streptavidin [4,5] and avidin  have been determined and revealed them to share a common fold: an eight stranded anti-parallel β-barrel with a repeated +1 topology enclosing an internal ligand binding site (see <PDB:1AVD>).
As a signature sequence for the avidin-like domain we selected a conserved motif located in its C-terminal section. We also developed a profile that covers the entire avidin-like domain.Note:
It is suggested, on the basis of similarities of structure, function, and sequence, that this family forms an overall superfamily, called the calycins, with the lipocalin <PDOC00187> and the cytosolic fatty-acid binding proteins <PDOC00188> families [7,8].Expert(s) to contact by email:
August 2007 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|Title||Avidin and streptavidin.|
|Source||Methods Enzymol. 184:51-67(1990).|
|2||Authors||Bisgrove B.W. Raff R.A.|
|Title||The SpEGF III gene encodes a member of the fibropellins: EGF repeat-containing proteins that form the apical lamina of the sea urchin embryo.|
|Source||Dev. Biol. 157:526-538(1993).|
|3||Authors||Yanai I. Yu Y. Zhu X. Cantor C.R. Weng Z.|
|Title||An avidin-like domain that does not bind biotin is adopted for oligomerization by the extracellular mosaic protein fibropellin.|
|Source||Protein. Sci. 14:417-423(2005).|
|4||Authors||Hendrickson W.A. Pahler A. Smith J.L. Satow Y. Merritt E.A. Phizackerley R.P.|
|Title||Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 86:2190-2194(1989).|
|5||Authors||Pugliese L. Coda A. Malcovati M. Bolognesi M.|
|Title||Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution.|
|Source||J. Mol. Biol. 231:698-710(1993).|
|6||Authors||Hunt L.T. Barker W.C.|
|Title||Avidin-like domain in an epidermal growth factor homolog from a sea urchin.|
|Source||FASEB J. 3:1760-1764(1989).|
|Title||Structural relationship of streptavidin to the calycin protein superfamily.|
|Source||FEBS Lett. 333:99-102(1993).|
|8||Authors||Holm L. Sander C.|
|Title||Searching protein structure databases has come of age.|