3MYU

Mycoplasma genitalium MG289

Summary for 3MYU

• Entry DOI: 10.2210/pdb3myu/pdb
• Related: 3e78 3e79 3eki
• Descriptor: High affinity transport system protein p37, 3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-ETHYL)-4-METHYL-THIAZOL-3-IUM, ACETATE ION, ... (4 entities in total)
• Functional Keywords: mycoplasma, mycoplasma genitalium, mg289, p37, g37, cypl, extracytoplasmic, thiamine binding protein, lipoprotein, atp binding cassette transporter binding protein, vib binding protein
• Biological source: Mycoplasma genitalium
• Cellular location: Cell membrane; Lipid-anchor: Q49410
• Total number of polymer chains: 2
• Total formula weight: 79753.92

Authors

Sippel, K.H.,Boehlein, S.K.,Govindasamy, L.,Namiki, K.,Satai, Y.,Quirit, J.G.,Agbandje-McKenna, M.,Goodison, S.,Rosser, C.J.,Sankaran, B.,McKenna, R. (deposition date: 2010-05-11, release date: 2010-10-20, Last modification date: 2023-09-06)

Primary citation

Sippel, K.H.,Venkatakrishnan, B.,Boehlein, S.K.,Sankaran, B.,Quirit, J.G.,Govindasamy, L.,Agbandje-McKenna, M.,Goodison, S.,Rosser, C.J.,McKenna, R.
Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein.
Proteins, 79:528-536, 2011

PubMed 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.

PubMed: 21117240
DOI: 10.1002/prot.22900

Experimental method

X-RAY DIFFRACTION (1.95 Å)