Structural highlights
Function
ACTH_THEAC Polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A. Crystal structure of an archaeal actin homolog. J Mol Biol. 2006 Apr 21;358(1):145-56. Epub 2006 Feb 9. PMID:16500678 doi:10.1016/j.jmb.2006.01.096
- ↑ Hara F, Yamashiro K, Nemoto N, Ohta Y, Yokobori S, Yasunaga T, Hisanaga S, Yamagishi A. An actin homolog of the archaeon Thermoplasma acidophilum that retains the ancient characteristics of eukaryotic actin. J Bacteriol. 2007 Mar;189(5):2039-45. Epub 2006 Dec 22. PMID:17189356 doi:http://dx.doi.org/JB.01454-06
