2mvj | pdb_00002mvj

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

spinqualitylabelsall models 2mvj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mvj is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPOVM_BACSU Coordinates cortex and coat assembly during sporulation (PubMed:22463703, PubMed:8231808). Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface (PubMed:17427285). May also serve as a competitive inhibitor of FtsH activity during sporulation (PubMed:9287010). Publication Abstract from PubMed 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 (SpoVMP9A) to reveal that SpoVM's atypical amphipathic alpha-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. Structural basis for the geometry-driven localization of a small protein.,Gill RL Jr, Castaing JP, Hsin J, Tan IS, Wang X, Huang KC, Tian F, Ramamurthi KS Proc Natl Acad Sci U S A. 2015 Mar 30. pii: 201423868. PMID:25825747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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