7ZPU

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

Summary for 7ZPU

• Entry DOI: 10.2210/pdb7zpu/pdb
• Related: 7ZPT 8AAM 8AB4
• Descriptor: Cell shape-determining protein MreB, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: structural protein, bacterial actin, bacterial cytoskeleton
• Biological source: Geobacillus stearothermophilus ATCC 7953
• Total number of polymer chains: 1
• Total formula weight: 36952.19

Authors

Li de la Sierra-Gallay, I.,Mao, W. (deposition date: 2022-04-28, release date: 2023-05-10, Last modification date: 2024-08-14)

Primary citation

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

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: 37818717
DOI: 10.7554/eLife.84505

Experimental method

X-RAY DIFFRACTION (1.96 Å)