2MVJ

Structure of Stage V sporulation protein M (SpoVM) P9A mutant

2MVJ の概要

• エントリーDOI: 10.2210/pdb2mvj/pdb
• 関連するPDBエントリー: 2MVH
• NMR情報: BMRB: 25270
• 分子名称: Stage V sporulation protein M (1 entity in total)
• 機能のキーワード: membrane protein, membrane curvature, protein binding
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2997.71

構造登録者

Tian, F.,Gill Jr., R. (登録日: 2014-10-07, 公開日: 2015-04-01, 最終更新日: 2024-05-15)

主引用文献

Gill, R.L.,Castaing, J.P.,Hsin, J.,Tan, I.S.,Wang, X.,Huang, K.C.,Tian, F.,Ramamurthi, K.S.
Structural basis for the geometry-driven localization of a small protein.
Proc.Natl.Acad.Sci.USA, 112:E1908-E1915, 2015

PubMed Abstract: In bacteria, certain shape-sensing proteins localize to differently curved membranes. During sporulation in Bacillus subtilis, the only convex (positively curved) surface in the cell is the forespore, an approximately spherical internal organelle. Previously, we demonstrated that SpoVM localizes to the forespore by preferentially adsorbing onto slightly convex membranes. Here, we used NMR and molecular dynamics simulations of SpoVM and a localization mutant (SpoVM(P9A)) to reveal that SpoVM's atypical amphipathic α-helix inserts deeply into the membrane and interacts extensively with acyl chains to sense packing differences in differently curved membranes. Based on binding to spherical supported lipid bilayers and Monte Carlo simulations, we hypothesize that SpoVM's membrane insertion, along with potential cooperative interactions with other SpoVM molecules in the lipid bilayer, drives its preferential localization onto slightly convex membranes. Such a mechanism, which is distinct from that used by high curvature-sensing proteins, may be widely conserved for the localization of proteins onto the surface of cellular organelles.

PubMed: 25825747
DOI: 10.1073/pnas.1423868112

実験手法

SOLUTION NMR