7zpu | pdb_00007zpu

Crystal structure of MreB from Geobacillus stearothermophilus ATCC7953 in complex with ATP

spinqualitylabelsall models 7zpu, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zpu is a 1 chain structure with sequence from Geobacillus stearothermophilus ATCC 7953. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.96Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A150MJ77_GEOSE Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature.[HAMAP-Rule:MF_02207] Publication Abstract from PubMed In vivo, bacterial actin MreB assembles into dynamic membrane-associated filamentous structures that exhibit circumferential motion around the cell. Current knowledge of MreB biochemical and polymerization properties in vitro remains limited and is mostly based on MreB proteins from Gram-negative species. In this study, we report the first observation of organized protofilaments by electron microscopy and the first 3D-structure of MreB from a Gram-positive bacterium. We show that Geobacillus stearothermophilus MreB forms straight pairs of protofilaments on lipid surfaces in the presence of ATP or GTP, but not in the presence of ADP, GDP or non-hydrolysable ATP analogs. We demonstrate that membrane anchoring is mediated by two spatially close short hydrophobic sequences while electrostatic interactions also contribute to lipid binding, and show that the population of membrane-bound protofilament doublets is in steady-state. In solution, protofilament doublets were not detected in any condition tested. Instead, MreB formed large sheets regardless of the bound nucleotide, albeit at a higher critical concentration. Altogether, our results indicate that both lipids and ATP are facilitators of MreB polymerization, and are consistent with a dual effect of ATP hydrolysis, in promoting both membrane binding and filaments assembly/disassembly. On the role of nucleotides and lipids in the polymerization of the actin homolog MreB from a Gram-positive bacterium.,Mao W, Renner LD, Cornilleau C, Li de la Sierra-Gallay I, Afensiss S, Benlamara S, Ah-Seng Y, Van Tilbeurgh H, Nessler S, Bertin A, Chastanet A, Carballido-Lopez R Elife. 2023 Oct 11;12:e84505. doi: 10.7554/eLife.84505. PMID:37818717 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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