1STP

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Summary for 1STP

• Entry DOI: 10.2210/pdb1stp/pdb
• Descriptor: STREPTAVIDIN COMPLEX WITH BIOTIN, BIOTIN (3 entities in total)
• Functional Keywords: biotin binding protein
• Biological source: Streptomyces avidinii
• Cellular location: Secreted: P22629
• Total number of polymer chains: 1
• Total formula weight: 16749.16

Authors

Weber, P.C.,Salemme, F.R. (deposition date: 1992-03-12, release date: 1992-10-15, Last modification date: 2024-02-14)

Primary citation

Weber, P.C.,Ohlendorf, D.H.,Wendoloski, J.J.,Salemme, F.R.
Structural origins of high-affinity biotin binding to streptavidin.
Science, 243:85-88, 1989

PubMed Abstract: The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.

PubMed: 2911722

Experimental method

X-RAY DIFFRACTION (2.6 Å)