Choukate, Komal and Chaudhuri, Barnali (2020) Structural basis of self-assembly in the lipid-binding domain of mycobacterial polar growth factor Wag31. IUCRJ, 7 (4). pp. 767-776.
Full text not available from this repository. (Request a copy)Abstract
Wag31, or DivIVA, is an essential protein and a drug target in the human pathogen Mycobacterium tuberculosis that self-assembles at the negatively curved membrane surface to form a higher-order structural scaffold, maintains rod-shaped cellular morphology and localizes key cell-wall synthesizing enzymes at the pole for exclusive polar growth. The crystal structure of the N-terminal lipid-binding domain of mycobacterial Wag31 was determined at 2.3 angstrom resolution. The structure revealed a highly polar surface lined with several conserved charged residues that suggest probable sites for interactions with membrane lipids. Crystal-packing analysis revealed a previously unseen `dimer-of-dimers' assembly state of N-terminal Wag31, which is formed by antiparallel stacking of two coiled-coil dimers. Size-exclusion column-chromatography-coupled small-angle solution X-ray scattering data revealed a tetrameric form as a major assembly state of N-terminal Wag31 in solution, further supporting the crystal structure. The results suggest that, in addition to lipid binding, the N-terminal Wag31 can participate in self-assembly to form filamentous structures. Plausible models of linear self-assembly and branching of Wag31 filaments consistent with available data are suggested.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to INT UNION CRYSTALLOGRAPHY. |
| Uncontrolled Keywords: | mycobacterial polar growth; dimer assembly; mycobacterium tuberculosis; coiled coil; lipids; filaments |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 29 Jul 2020 10:19 |
| Last Modified: | 29 Jul 2020 10:19 |
| URI: | http://crdd.osdd.net/open/id/eprint/2586 |
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