Structural highlights
Function
[PARM_ECOLX] Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Segregation of the R1 plasmid in bacteria relies on ParM, an actin homolog that segregates plasmids by switching between cycles of polymerization and depolymerization. We find similar polymerization kinetics and stability in the presence of either ATP or GTP and a 10-fold affinity preference for ATP over GTP. We used electron cryo-microscopy to evaluate the heterogeneity within ParM filaments. In addition to variable twist, ParM has variable axial rise, and both parameters are coupled. Subunits in the same ParM filaments can exist in two different structural states, with the nucleotide-binding cleft closed or open, and the bound nucleotide biases the distribution of states. The interface between protomers is different between these states, and in neither state is it similar to F-actin. Our results suggest that the closed state of the cleft is required but not sufficient for ParM polymerization, and provide a structural basis for the dynamic instability of ParM filaments.
Structural polymorphism of the ParM filament and dynamic instability.,Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH Structure. 2009 Sep 9;17(9):1253-64. PMID:19748346[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH. Structural polymorphism of the ParM filament and dynamic instability. Structure. 2009 Sep 9;17(9):1253-64. PMID:19748346 doi:10.1016/j.str.2009.07.008
