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Archaeal actin homologue MreB-like, C-terminal
Archaeal actin homologue Ta0583 is an active ATPase at physiological temperatures, which has a propensity to form filaments [1]. It has the core actin structure and is highly homologous to MreB and ParM from bacteria [1,2]. This entry represents the C-terminal actin-like domain [1,2]. Paper describing PDB structure 2fsj. [1]. 16500678. Crystal structure of an archaeal actin homolog. Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A;. J Mol Biol. 2006;358:145-156. [2]. 20106979. Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation. Popp D, Xu W, Narita A, Brzoska AJ, Skurray RA, Firth N, Goshdastider U, Maeda Y, Robinson RC, Schumacher MA;. J Biol Chem. 2010;285:10130-10140. (from Pfam)
Plasmid segregation protein ParM, C-terminal
This entry consists of several bacterial ParM/StbA plasmid stability proteins [1-3]. ParM is involved in the control of plasmid partition and required for the accurate segregation of the plasmid, which forms filaments to drive partition. This protein is an actin homologue and consists of two domains (I and II) with the same conformation [1-3]. This entry represents the C-terminal domain. [1]. 16500678. Crystal structure of an archaeal actin homolog. Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A;. J Mol Biol. 2006;358:145-156. [2]. 20106979. Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation. Popp D, Xu W, Narita A, Brzoska AJ, Skurray RA, Firth N, Goshdastider U, Maeda Y, Robinson RC, Schumacher MA;. J Biol Chem. 2010;285:10130-10140. [3]. 19748346. Structural polymorphism of the ParM filament and dynamic instability. Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH;. Structure. 2009;17:1253-1264. (from Pfam)
plasmid segregation protein ParM domain-containing protein
This entry consists of several bacterial ParM/StbA plasmid stability proteins [1-3]. ParM is involved in the control of plasmid partition and required for the accurate segregation of the plasmid, which forms filaments to drive partition. This protein is an actin homologue and consists of two domains (I and II) with the same conformation [2-4]. This is the N-terminal domain. [1]. 1706707. Transcription of the stability operon of IncFII plasmid NR1. Min YN, Tabuchi A, Womble DD, Rownd RH;. J Bacteriol 1991;173:2378-2384. [2]. 16500678. Crystal structure of an archaeal actin homolog. Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A;. J Mol Biol. 2006;358:145-156. [3]. 20106979. Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation. Popp D, Xu W, Narita A, Brzoska AJ, Skurray RA, Firth N, Goshdastider U, Maeda Y, Robinson RC, Schumacher MA;. J Biol Chem. 2010;285:10130-10140. [4]. 19748346. Structural polymorphism of the ParM filament and dynamic instability. Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH;. Structure. 2009;17:1253-1264. (from Pfam)
plasmid segregation protein ParM
plasmid segregation protein ParM is involved in the control of plasmid partition, and is required for the accurate segregation of the plasmid
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