Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein

Katherine H. Sippel, Balasubramanian Venkatakrishnan, Susan K. Boehlein, Banumathi Sankaran, Jeanne G. Quirit, Lakshamanan Govindasamy, Mavis Agbandje-McKenna, Steven Goodison, Charles J. Rosser, Robert McKenna

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Mycoplasma genitalium is one of the smallest organisms capable of self-replication and its sequence is considered a starting point for understanding the minimal genome required for life. MG289, a putative phosphonate substrate binding protein, is considered to be one of these essential genes. The crystal structure of MG289 has been solved at 1.95 Å resolution. The structurally identified thiamine binding region reveals possible mechanisms for ligand promiscuity. MG289 was determined to be an extracytoplasmic thiamine binding lipoprotein. Computational analysis, size exclusion chromatography, and small angle X-ray scattering indicates that MG289 homodimerizes in a concentration-dependant manner. Comparisons to the thiamine pyrophosphate binding homolog Cypl reveal insights into the metabolic differences between mycoplasmal species including identifying possible kinases for cofactor phosphorylation and describing the mechanism of thiamine transport into the cell. These results provide a baseline to build our understanding of the minimal metabolic requirements of a living organism.

Original languageEnglish (US)
Pages (from-to)528-536
Number of pages9
JournalProteins: Structure, Function and Bioinformatics
Volume79
Issue number2
DOIs
StatePublished - Feb 1 2011
Externally publishedYes

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Mycoplasma genitalium
Thiamine
Metabolism
Lipoproteins
Genes
Thiamine Pyrophosphate
Organophosphonates
Phosphorylation
Size exclusion chromatography
Essential Genes
X ray scattering
Gel Chromatography
Carrier Proteins
Phosphotransferases
Crystal structure
X-Rays
Genome
Ligands
Substrates

Keywords

  • Cypl
  • Extracytoplasmic lipoprotein
  • P37
  • Sexually transmitted infection
  • Small angle X-ray scattering
  • Substrate binding protein
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Cite this

Sippel, K. H., Venkatakrishnan, B., Boehlein, S. K., Sankaran, B., Quirit, J. G., Govindasamy, L., ... McKenna, R. (2011). Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein. Proteins: Structure, Function and Bioinformatics, 79(2), 528-536. https://doi.org/10.1002/prot.22900

Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein. / Sippel, Katherine H.; Venkatakrishnan, Balasubramanian; Boehlein, Susan K.; Sankaran, Banumathi; Quirit, Jeanne G.; Govindasamy, Lakshamanan; Agbandje-McKenna, Mavis; Goodison, Steven; Rosser, Charles J.; McKenna, Robert.

In: Proteins: Structure, Function and Bioinformatics, Vol. 79, No. 2, 01.02.2011, p. 528-536.

Research output: Contribution to journalArticle

Sippel, KH, Venkatakrishnan, B, Boehlein, SK, Sankaran, B, Quirit, JG, Govindasamy, L, Agbandje-McKenna, M, Goodison, S, Rosser, CJ & McKenna, R 2011, 'Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein', Proteins: Structure, Function and Bioinformatics, vol. 79, no. 2, pp. 528-536. https://doi.org/10.1002/prot.22900
Sippel, Katherine H. ; Venkatakrishnan, Balasubramanian ; Boehlein, Susan K. ; Sankaran, Banumathi ; Quirit, Jeanne G. ; Govindasamy, Lakshamanan ; Agbandje-McKenna, Mavis ; Goodison, Steven ; Rosser, Charles J. ; McKenna, Robert. / Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein. In: Proteins: Structure, Function and Bioinformatics. 2011 ; Vol. 79, No. 2. pp. 528-536.
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