2bc3
|
T7-tagged full-length streptavidin
OverviewOverview
The structure of a full-length streptavidin has been determined at 1.7 A resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150-153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity.
About this StructureAbout this Structure
2BC3 is a Single protein structure of sequence from Streptomyces avidinii with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic analysis of a full-length streptavidin with its C-terminal polypeptide bound in the biotin binding site., Le Trong I, Humbert N, Ward TR, Stenkamp RE, J Mol Biol. 2006 Feb 24;356(3):738-45. Epub 2005 Dec 15. PMID:16384581
Page seeded by OCA on Thu Feb 21 16:36:18 2008