2WIU

Mercury-modified bacterial persistence regulator hipBA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.218 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

New Kinase Regulation Mechanism Found in Hipba: A Bacterial Persistence Switch.

Evdokimov, A., Voznesensky, I., Fennell, K., Anderson, M., Smith, J.F., Fisher, D.A.

(2009) Acta Crystallogr D Biol Crystallogr 65: 875

  • DOI: https://doi.org/10.1107/S0907444909018800
  • Primary Citation of Related Structures:  
    2WIU

  • PubMed Abstract: 

    Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data.

    • Organizational Affiliation: 

    Pfizer Inc, Groton, Connecticut, USA. artem@xtals.org


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN HIPA
A, C
446Escherichia coliMutation(s): 0 
EC: 2.7.11.1
UniProt
Find proteins for P23874 (Escherichia coli (strain K12))
Explore P23874 
Go to UniProtKB:  P23874
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23874
Sequence Annotations
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  • Reference Sequence
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(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
HTH-TYPE TRANSCRIPTIONAL REGULATOR HIPB
B, D
88Escherichia coliMutation(s): 0 
UniProt
Find proteins for P23873 (Escherichia coli (strain K12))
Explore P23873 
Go to UniProtKB:  P23873
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23873
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HG
Query on HG
Download Ideal Coordinates CCD File 
E [auth A]
F [auth A]
J [auth B]
M [auth C]
N [auth C]
E [auth A],
F [auth A],
J [auth B],
M [auth C],
N [auth C],
O [auth C],
S [auth D]
MERCURY (II) ION
Hg
BQPIGGFYSBELGY-UHFFFAOYSA-N
CL
Query on CL
Download Ideal Coordinates CCD File 
G [auth A]
H [auth A]
I [auth A]
K [auth B]
L [auth B]
G [auth A],
H [auth A],
I [auth A],
K [auth B],
L [auth B],
P [auth C],
Q [auth C],
R [auth C],
T [auth D],
U [auth D]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.218 
  • Space Group: P 42 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 166.933α = 90
b = 166.933β = 90
c = 124.577γ = 90
Software Package:
Software NamePurpose
HKL-2000data reduction
SCALEPACKdata scaling
SHARPphasing
SOLOMONphasing
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-07-28
    Type: Initial release
  • Version 1.1: 2012-04-04
    Changes: Database references, Derived calculations, Non-polymer description, Other, Refinement description, Structure summary, Version format compliance