2WUS

Bacterial actin MreB assembles in complex with cell shape protein RodZ

Summary for 2WUS

• Entry DOI: 10.2210/pdb2wus/pdb
• Related: 1JCE 1JCF 1JCG
• Descriptor: ROD SHAPE-DETERMINING PROTEIN MREB, PUTATIVE UNCHARACTERIZED PROTEIN (2 entities in total)
• Functional Keywords: structural protein, cell wall morphogenesis, bacterial cytoskeleton, bacterial actin, helix-turn-helix motif
• Biological source: THERMOTOGA MARITIMA; More
• Total number of polymer chains: 4
• Total formula weight: 100623.98

Authors

van den Ent, F.,Johnson, C.M.,Persons, L.,deBoer, P.,Lowe, J. (deposition date: 2009-10-08, release date: 2010-06-30, Last modification date: 2023-12-20)

Primary citation

van den Ent, F.,Johnson, C.M.,Persons, L.,deBoer, P.,Lowe, J.
Bacterial Actin Mreb Assembles in Complex with Cell Shape Protein Rodz.
Embo J., 29:1081-, 2010

PubMed Abstract: Bacterial actin homologue MreB is required for cell shape maintenance in most non-spherical bacteria, where it assembles into helical structures just underneath the cytoplasmic membrane. Proper assembly of the actin cytoskeleton requires RodZ, a conserved, bitopic membrane protein that colocalises to MreB and is essential for cell shape determination. Here, we present the first crystal structure of bacterial actin engaged with a natural partner and provide a clear functional significance of the interaction. We show that the cytoplasmic helix-turn-helix motif of Thermotoga maritima RodZ directly interacts with monomeric as well as filamentous MreB and present the crystal structure of the complex. In vitro and in vivo analyses of mutant T. maritima and Escherichia coli RodZ validate the structure and reveal the importance of the MreB-RodZ interaction in the ability of cells to propagate as rods. Furthermore, the results elucidate how the bacterial actin cytoskeleton might be anchored to the membrane to help constrain peptidoglycan synthesis in the periplasm.

PubMed: 20168300
DOI: 10.1038/EMBOJ.2010.9

Experimental method

X-RAY DIFFRACTION (2.9 Å)