7r1c

Cryo-EM structure of Bacillus megaterium gas vesicles

spinqualitylabelsall models 7r1c, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7r1c is a 1 chain structure with sequence from Priestia megaterium NBRC 15308 = ATCC 14581. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0B6AAV2_PRIM2 Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell.[HAMAP-Rule:MF_00576][RuleBase:RU000632] Publication Abstract from PubMed Gas vesicles are gas-filled nanocompartments that allow a diverse group of bacteria and archaea to control their buoyancy. The molecular basis of their properties and assembly remains unclear. Here, we report the 3.2 A cryo-EM structure of the gas vesicle shell made from the structural protein GvpA that self-assembles into hollow helical cylinders closed off by cone-shaped tips. Two helical half shells connect through a characteristic arrangement of GvpA monomers, suggesting a mechanism of gas vesicle biogenesis. The fold of GvpA features a corrugated wall structure typical for force-bearing thin-walled cylinders. Small pores enable gas molecules to diffuse across the shell, while the exceptionally hydrophobic interior surface effectively repels water. Comparative structural analysis confirms the evolutionary conservation of gas vesicle assemblies and demonstrates molecular features of shell reinforcement by GvpC. Our findings will further research into gas vesicle biology and facilitate molecular engineering of gas vesicles for ultrasound imaging. Cryo-EM structure of gas vesicles for buoyancy-controlled motility.,Huber ST, Terwiel D, Evers WH, Maresca D, Jakobi AJ Cell. 2023 Mar 2;186(5):975-986.e13. doi: 10.1016/j.cell.2023.01.041. PMID:36868215 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA