6BEK

Structure of sIHF bound to an 8bp palindromic DNA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Streptomyces IHF uses multiple interfaces to bind DNA.

Nanji, T., Gehrke, E.J., Shen, Y., Gloyd, M., Zhang, X., Firby, C.D., Huynh, A., Razi, A., Ortega, J., Elliot, M.A., Guarne, A.

(2019) Biochim Biophys Acta Gen Subj 1863: 129405-129405

  • DOI: https://doi.org/10.1016/j.bbagen.2019.07.014
  • Primary Citation of Related Structures:  
    6BEK

  • PubMed Abstract: 

    Nucleoid associated proteins (NAPs) are essential for chromosome condensation in bacterial cells. Despite being a diverse group, NAPs share two common traits: they are small, oligomeric proteins and their oligomeric state is critical for DNA condensation. Streptomyces coelicolor IHF (sIHF) is an actinobacterial-specific nucleoid-associated protein that despite its name, shares neither sequence nor structural homology with the well-characterized Escherichia coli IHF. Like E. coli IHF, sIHF is needed for efficient nucleoid condensation, morphological development and antibiotic production in S. coelicolor.

    • Organizational Affiliation: 

    Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON, Canada.


Macromolecules

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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SCO1480
A, D
107Streptomyces coelicolorMutation(s): 0 
Gene Names: SCO1480
UniProt
Find proteins for Q9KXR9 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
Explore Q9KXR9 
Go to UniProtKB:  Q9KXR9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KXR9
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(*CP*AP*TP*GP*CP*AP*TP*G)-3')
B, C, E, F
8Escherichia coli
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.26α = 90
b = 72.11β = 90
c = 103.257γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-10-31
    Type: Initial release
  • Version 1.1: 2019-09-25
    Changes: Data collection, Database references
  • Version 1.2: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description