7ZPT
Crystal structure of MreB from Geobacillus stearothermophilus ATCC7953
7ZPT の概要
エントリーDOI | 10.2210/pdb7zpt/pdb |
分子名称 | Cell shape-determining protein MreB, PENTAETHYLENE GLYCOL (3 entities in total) |
機能のキーワード | structural protein, bacterial actin, bacterial cytoskeleton |
由来する生物種 | Geobacillus stearothermophilus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 36683.29 |
構造登録者 | |
主引用文献 | Mao, W.,Renner, L.D.,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. On the role of nucleotides and lipids in the polymerization of the actin homolog MreB from a Gram-positive bacterium. Elife, 12:-, 2023 Cited by PubMed Abstract: 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 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 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. PubMed: 37818717DOI: 10.7554/eLife.84505 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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