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Crystallographic Analysis of a Full-length Streptavidin with Its C-terminal Polypeptide Bound in the Biotin Binding Site
- Source :
- Journal of Molecular Biology. 356:738-745
- Publication Year :
- 2006
- Publisher :
- Elsevier BV, 2006.
-
Abstract
- The structure of a full-length streptavidin has been determined at 1.7 Å 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.
- Subjects :
- Streptavidin
Biotin binding
Strep-tag
Molecular Sequence Data
Biotin
Crystallography, X-Ray
010402 general chemistry
01 natural sciences
03 medical and health sciences
chemistry.chemical_compound
Protein structure
Tetramer
Structural Biology
Amino Acid Sequence
Binding site
Molecular Biology
030304 developmental biology
0303 health sciences
Binding Sites
Water
Peptide Fragments
Streptomyces
Protein Structure, Tertiary
0104 chemical sciences
3. Good health
Crystallography
chemistry
Biotinylation
Protein Binding
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 356
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....8bc25cafb8bf9eb4a91b58efaec760e9