2.7.7.72	?	x * 48000, SDS-PAGE	721043	
2.7.7.72	dimer	2 * 48000, the 48 kDa monomer forms a stable salt-resistant dimer in solution. Further dimerization of the dimeric enzyme to form a tetramer is induced by the binding of two tRNA molecules	720225	
2.7.7.72	monomer	1 * 51500, SDS-PAGE	-, 643030	
2.7.7.72	additional information	class 1 enzymes have a tRNA-binding body domain consisting of a beta sheet with flanking alpha helices. Head and neck domains form the active site and are also composed of alpha-helical and beta-sheet elements, structure-function relationship, overview	722263	
2.7.7.72	additional information	class II enzymes found in bacteria and eukaryotes carry a flexible loop in their catalytic core required for switching the specificity of the nucleotide binding pocket from CTP- to ATP-recognition, with the existence of conserved loop families. Loop replacements within families do not interfere with enzymatic activity. Modeling experiments suggest specific interactions of loop positions with important elements of the protein, forming a lever-like structure	710150	
2.7.7.72	additional information	four domain architecture with a cluster of conserved residues forming a positively charged cleft between the first two domains, modeling of human mitochondrial tRNA-nucleotidyltransferase monomer	643052	
2.7.7.72	additional information	in class 2 enzymes, only the head domain carries a beta-sheet and forms the nucleotidyltransferase core, while neck, body and tail consist exclusively of alpha helices, giving the enzyme a hook- or seahorse-like overall structure, structure-function relationship, overview	722263	
2.7.7.72	additional information	the enzyme comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain	652555	
2.7.7.72	tetramer	2 * 48000, the 48 kDa monomer forms a stable salt-resistant dimer in solution. Further dimerization of the dimeric enzyme to form a tetramer is induced by the binding of two tRNA molecules	720225