2MVH

Structure determination of Stage V sporulation protein M (SpoVM)

Summary for 2MVH

• Entry DOI: 10.2210/pdb2mvh/pdb
• Related: 2MVJ
• NMR Information: BMRB: 25268
• Descriptor: Stage V sporulation protein M (1 entity in total)
• Functional Keywords: spovm, protein binding
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 3023.75

Authors

Tian, F.,Gill Jr., R. (deposition date: 2014-10-06, release date: 2015-04-01, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR