@article{open2503,
           month = {November},
          author = {Komal Choukate and Aanchal Gupta and Brohmomoy Basu and Karman Virk and Munia Ganguli and Barnali Chaudhuri},
            note = {Copyright of this article belongs to Elsevier Science },
           title = {Higher order assembling of the mycobacterial polar growth factor DivIVA/Wag31.},
       publisher = {Elsevier Science },
         journal = {Journal of structural biology},
           pages = {107429},
            year = {2019},
        keywords = {AFM; DivIVA; Mycobacterial growth; SAXS; Wag31 filament; bacterial polar growth

},
             url = {http://crdd.osdd.net/open/2503/},
        abstract = {DivIVA or Wag31, which is an essential pole organizing protein in mycobacteria, can self-assemble at the negatively curved side of the membrane at the growing pole to form a higher order structural scaffold for maintaining cellular morphology and localizing various target proteins for cell-wall biogenesis. The structural organization of polar scaffold formed by polymerization of coiled-coil rich Wag31, which is implicated in the anti-tubercular activities of amino-pyrimidine sulfonamides, remains to be determined. A single-site phosphorylation in Wag31 regulates peptidoglycan biosynthesis in mycobacteria. We report biophysical characterizations of filaments formed by mycobacterial Wag31 using circular dichroism, atomic force microscopy and small angle solution X-ray scattering. Atomic force microscopic images of the wild-type, a phospho-mimetic (T73E) and a phospho-ablative (T73A) form of Wag31 show mostly linear filament formation with occasional curving, kinking and apparent branching. Solution X-ray scattering data indicates that the phospho-mimetic forms of the Wag31 polymers are on average more compact than their phospho-ablative counterparts, which is likely due to the extent of bending/branching. Observed structural features in this first view of Wag31 filaments suggest a basis for higher order Wag31 scaffold formation at the pole.}
}