1stp

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spinqualitylabelsall models PDB ID 1stp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1stp, resolution 2.60Å ()
Ligands:
Structural annotation: Resources: CATH : 1Stp000 InterPro : Ipr005469, Ipr005468 Pfam : PF01382 SCOP : d1stp__ UniProt : P22629
Evolutionary conservation: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Overview

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.

About this Structure

1STP is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.

Reference

Structural origins of high-affinity biotin binding to streptavidin., Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR, Science. 1989 Jan 6;243(4887):85-8. PMID:2911722