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Features critical for membrane binding revealed by DivIVA crystal structure

Lookup NU author(s): Dr Sven Halbedel, Dr Leendert Hamoen


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DivIVA is a conserved protein in Gram-positive bacteria that localizes at the poles and division sites, presumably through direct sensing of membrane curvature. DivIVA functions as a scaffold and is vital for septum site selection during vegetative growth and chromosome anchoring during sporulation. DivIVA deletion causes filamentous growth in Bacillus subtilis, whereas overexpression causes hyphal branching in Streptomyces coelicolor. We have determined the crystal structure of the N-terminal (Nt) domain of DivIVA, and show that it forms a parallel coiled-coil. It is capped with two unique crossed and intertwined loops, exposing hydrophobic and positively charged residues that we show here are essential for membrane binding. An intragenic suppressor introducing a positive charge restores membrane binding after mutating the hydrophobic residues. We propose that the hydrophobic residues insert into the membrane and that the positively charged residues bind to the membrane surface. A low-resolution crystal structure of the C-terminal (Ct) domain displays a curved tetramer made from two parallel coiled-coils. The Nt and Ct parts were then merged into a model of the full length, 30 nm long DivIVA protein. The EMBO Journal (2010) 29, 1988-2001. doi: 10.1038/emboj.2010.99; Published online 25 May 2010

Publication metadata

Author(s): Oliva MA, Halbedel S, Freund SM, Dutow P, Leonard TA, Veprintsev DB, Hamoen LW, Lowe J

Publication type: Article

Publication status: Published

Journal: EMBO Journal

Year: 2010

Volume: 29

Issue: 12

Pages: 1988-2001

Print publication date: 01/06/2010

ISSN (print): 0261-4189

ISSN (electronic): 1460-2075

Publisher: Nature Publishing Group


DOI: 10.1038/emboj.2010.99


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