TY - JOUR
T1 - Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein
AU - Sippel, Katherine H.
AU - Venkatakrishnan, Balasubramanian
AU - Boehlein, Susan K.
AU - Sankaran, Banumathi
AU - Quirit, Jeanne G.
AU - Govindasamy, Lakshamanan
AU - Agbandje-McKenna, Mavis
AU - Goodison, Steve
AU - Rosser, Charles J.
AU - McKenna, Robert
PY - 2011/2
Y1 - 2011/2
N2 - 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.
AB - 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.
KW - Cypl
KW - Extracytoplasmic lipoprotein
KW - P37
KW - Sexually transmitted infection
KW - Small angle X-ray scattering
KW - Substrate binding protein
KW - X-ray crystallography
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U2 - 10.1002/prot.22900
DO - 10.1002/prot.22900
M3 - Article
C2 - 21117240
AN - SCOPUS:78650780137
SN - 0887-3585
VL - 79
SP - 528
EP - 536
JO - Proteins: Structure, Function and Bioinformatics
JF - Proteins: Structure, Function and Bioinformatics
IS - 2
ER -