2WUK

DivIVA N-terminal domain, F17A mutant

2WUK の概要

• エントリーDOI: 10.2210/pdb2wuk/pdb
• 関連するPDBエントリー: 2WUJ
• 分子名称: SEPTUM SITE-DETERMINING PROTEIN DIVIVA (2 entities in total)
• 機能のキーワード: bacterial cell division, septation, cell cycle, sporulation
• 由来する生物種: BACILLUS SUBTILIS
• 細胞内の位置: Cytoplasm: P71021
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 27050.35

構造登録者

Oliva, M.A.,Leonard, T.A.,Lowe, J. (登録日: 2009-10-06, 公開日: 2010-06-09, 最終更新日: 2024-05-08)

主引用文献

Oliva, M.A.,Halbedel, S.,Freund, S.M.,Dutow, P.,Leonard, T.A.,Veprintsev, D.B.,Hamoen, L.W.,Lowe, J.
Features Critical for Membrane Binding Revealed by Diviva Crystal Structure.
Embo J., 29:1988-, 2010

PubMed Abstract: 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.

PubMed: 20502438
DOI: 10.1038/EMBOJ.2010.99

実験手法

X-RAY DIFFRACTION (1.9 Å)