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Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae.

Publication ,  Journal Article
Steinhauer, K; Allen, GS; Hillen, W; Stülke, J; Brennan, RG
Published in: Acta Crystallogr D Biol Crystallogr
March 2002

The Mycoplasma pneumoniae HPr kinase/phosphatase (HPrK/P) is a member of a large family of enzymes which are central to carbon regulation in Gram-positive bacteria. The full-length M. pneumonia HPrK/P was crystallized from solutions of polyethylene glycol 8000 and KCl or NaCl which also contained the non-hydrolysable ATP analog adenosine 5'-[beta, gamma-methylene]triphosphate (AMPPCP). The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 117.1, b = 127.7, c = 170.7 A. A complete X-ray intensity data set has been collected and processed to 2.50 A resolution. The slow self-rotation function revealed the presence of a sixfold axis. Dynamic light-scattering (DLS) experiments indicated a molecular weight of 197 kDa for HPrK/P in the absence of AMPPCP and of 217 kDa in the presence of the ATP analog. Thus, the biophysical and crystallographic data suggest that HPrK/P is a functional hexamer that undergoes an ATP-binding-induced conformational change.

Duke Scholars

Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

March 2002

Volume

58

Issue

Pt 3

Start / End Page

515 / 518

Location

United States

Related Subject Headings

  • Titrimetry
  • Protein Serine-Threonine Kinases
  • Protein Conformation
  • Mycoplasma pneumoniae
  • Models, Molecular
  • Dithionitrobenzoic Acid
  • Crystallography, X-Ray
  • Crystallization
  • Biophysics
  • Bacterial Proteins
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Steinhauer, K., Allen, G. S., Hillen, W., Stülke, J., & Brennan, R. G. (2002). Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae. Acta Crystallogr D Biol Crystallogr, 58(Pt 3), 515–518. https://doi.org/10.1107/s090744490102145x
Steinhauer, Katrin, Gregory S. Allen, Wolfgang Hillen, Jörg Stülke, and Richard G. Brennan. “Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae.Acta Crystallogr D Biol Crystallogr 58, no. Pt 3 (March 2002): 515–18. https://doi.org/10.1107/s090744490102145x.
Steinhauer K, Allen GS, Hillen W, Stülke J, Brennan RG. Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae. Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):515–8.
Steinhauer, Katrin, et al. “Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae.Acta Crystallogr D Biol Crystallogr, vol. 58, no. Pt 3, Mar. 2002, pp. 515–18. Pubmed, doi:10.1107/s090744490102145x.
Steinhauer K, Allen GS, Hillen W, Stülke J, Brennan RG. Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae. Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):515–518.

Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

March 2002

Volume

58

Issue

Pt 3

Start / End Page

515 / 518

Location

United States

Related Subject Headings

  • Titrimetry
  • Protein Serine-Threonine Kinases
  • Protein Conformation
  • Mycoplasma pneumoniae
  • Models, Molecular
  • Dithionitrobenzoic Acid
  • Crystallography, X-Ray
  • Crystallization
  • Biophysics
  • Bacterial Proteins