1STP

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Observed: 0.220 

wwPDB Validation 3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural origins of high-affinity biotin binding to streptavidin.

Weber, P.C.Ohlendorf, D.H.Wendoloski, J.J.Salemme, F.R.

(1989) Science 243: 85-88

  • DOI: 10.1126/science.2911722
  • Structures With Same Primary Citation

  • 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 refine ...

    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.


    Related Citations: 
    • Crystallographic and Thermodynamic Comparison of Natural and Synthetic Ligands Bound to Streptavidin
      Weber, P.C., Wendoloski, J.J., Pantoliano, M.W., Salemme, F.R.
      (1992) J Am Chem Soc 114: 3197

    Organizational Affiliation

    Central Research & Development Department, E. I. du Pont de Neumours and Company, Inc., Wilmington, DE 19880-0228.



Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
STREPTAVIDIN COMPLEX WITH BIOTIN
A
159Streptomyces avidiniiMutation(s): 0 
Find proteins for P22629 (Streptomyces avidinii)
Go to UniProtKB:  P22629
Small Molecules
Ligands 1 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
BTN
Query on BTN

Download CCD File 
A
BIOTIN
C10 H16 N2 O3 S
YBJHBAHKTGYVGT-ZKWXMUAHSA-N
 Ligand Interaction
External Ligand Annotations 
IDBinding Affinity (Sequence Identity %)
BTNΔH:  123.01000213623047   kJ/mol  BindingDB
BTNΔH:  66.94000244140625   kJ/mol  BindingDB
BTNΔH:  115.05999755859375   kJ/mol  BindingDB
BTNΔH:  90.37000274658203   kJ/mol  BindingDB
BTNΔH:  89.95999908447266   kJ/mol  BindingDB
BTNKd :  0.000039999998989515007   nM  PDBBind
BTNΔH:  104.18000030517578   kJ/mol  BindingDB
BTNΔH:  100.41999816894531   kJ/mol  BindingDB
BTNΔH:  102.51000213623047   kJ/mol  BindingDB
BTNΔH:  97.48999786376953   kJ/mol  BindingDB
BTNΔH:  75.30999755859375   kJ/mol  BindingDB
BTNΔH:  117.98999786376953   kJ/mol  BindingDB
BTNΔH:  107.52999877929688   kJ/mol  BindingDB
BTNKd:  1   nM  BindingDB
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Observed: 0.220 
  • Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.4α = 90
b = 99.4β = 90
c = 125.8γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 1992-10-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance