2QU4

Model for Bacterial ParM Filament

Summary for 2QU4

Entry DOI	10.2210/pdb2qu4/pdb
Descriptor	Plasmid segregation protein parM (1 entity in total)
Functional Keywords	filament model, actin-like protein, helical polymer, plasmid, plasmid partition, structural protein
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	35804.38
Authors	Orlova, A.,Garner, E.C.,Galkin, V.E.,Heuser, J.,Mullins, R.D.,Egelman, E.H. (deposition date: 2007-08-03, release date: 2007-09-18, Last modification date: 2024-02-21)
Primary citation	Orlova, A.,Garner, E.C.,Galkin, V.E.,Heuser, J.,Mullins, R.D.,Egelman, E.H. The structure of bacterial ParM filaments. Nat.Struct.Mol.Biol., 14:921-926, 2007 Cited by PubMed Abstract: Bacterial ParM is a homolog of eukaryotic actin and is involved in moving plasmids so that they segregate properly during cell division. Using cryo-EM and three-dimensional reconstruction, we show that ParM filaments have a different structure from F-actin, with very different subunit-subunit interfaces. These interfaces result in the helical handedness of the ParM filament being opposite to that of F-actin. Like F-actin, ParM filaments have a variable twist, and we show that this involves domain-domain rotations within the ParM subunit. The present results yield new insights into polymorphisms within F-actin, as well as the evolution of polymer families. PubMed: 17873883 DOI: 10.1038/nsmb1300 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (16 Å)

Structure validation