2F01

Epi-biotin complex with core streptavidin

Summary for 2F01

• Entry DOI: 10.2210/pdb2f01/pdb
• Related: 1MK5
• Descriptor: Streptavidin, BIOTIN, EPI-BIOTIN, ... (5 entities in total)
• Functional Keywords: protein/ligand interactions, streptavidin, biotin, biotin binding protein
• Biological source: Streptomyces avidinii
• Cellular location: Secreted: P22629
• Total number of polymer chains: 2
• Total formula weight: 27816.20

Authors

Le Trong, I.,Aubert, D.G.,Thomas, N.R.,Stenkamp, R.E. (deposition date: 2005-11-10, release date: 2005-11-29, Last modification date: 2023-08-23)

Primary citation

Le Trong, I.,Aubert, D.G.,Thomas, N.R.,Stenkamp, R.E.
The high-resolution structure of (+)-epi-biotin bound to streptavidin.
Acta Crystallogr.,Sect.D, 62:576-581, 2006

PubMed Abstract: (+)-Epi-biotin differs from (+)-biotin in the configuration of the chiral center at atom C2. This could lead to a difference in the mode of binding of (+)-epi-biotin to streptavidin, a natural protein receptor for (+)-biotin. Diffraction data were collected to a maximum of 0.85 Angstrom resolution for structural analysis of the complex of streptavidin with a sample of (+)-epi-biotin and refinement was carried out at both 1.0 and 0.85 Angstrom resolution. The structure determination shows a superposition of two ligands in the binding site, (+)-biotin and (+)-epi-biotin. The molecules overlap in the model for the complex except for the position of S1 in the tetrahydrothiophene ring. Differences in the conformation of the ring permits binding of each molecule to streptavidin with little observable difference in the protein structures at this high resolution.

PubMed: 16699183
DOI: 10.1107/S0907444906011887

Experimental method

X-RAY DIFFRACTION (0.85 Å)