2.7.7.23	?	x * 49624, calculated from the deduced amino acid sequence of the His-tagged protein	661821	
2.7.7.23	?	x * 52922, calculated	-, 722855	
2.7.7.23	?	x * 52965, recombinant His6-tagged enzyme, SDS-PAGE and mass spectrometry	-, 735569	
2.7.7.23	?	x * 54071, wild-type SPL29, sequence calculation, x * 54117, mutant spl29, sequence calculation	-, 738765	
2.7.7.23	?	x * 54500, calculated from amino acid sequence	760749	
2.7.7.23	?	x * 55100, approximately, sequence calculation	739475	
2.7.7.23	?	x * 55800, approximately, sequence calculation	739475	
2.7.7.23	?	x * 58360, calculated from SDS-PAGE	760749	
2.7.7.23	?	x * 58360, recombinant His-tagged enzyme, SDS-PAGE	760749	
2.7.7.23	?	x * 60000, SDS-PAGE	721526	
2.7.7.23	dimer	1 * 64000 + 1 * 57000	643069	
2.7.7.23	dimer	2 * 33000, SDS-PAGE, gel filtration	643067	
2.7.7.23	dimer	2 * 64000, SDS-PAGE, gel filtration	643065	
2.7.7.23	hexamer	trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction	723724	
2.7.7.23	monomer	1 * 50000, SDS-PAGE, 1 * 49624, calculated from the deduced amino acid sequence, native mass by gel filtration	662429	
2.7.7.23	monomer	1 * 58300, SDS-PAGE	721526	
2.7.7.23	additional information	C324 does not form a disulphide bond with any other cysteine. This is consistent with the replacement of C307 by a serine in Y. pestis and the great distance between the three other cysteines (C296, C301 and C385) and C324	-, 735569	
2.7.7.23	additional information	the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1–210) and the C-terminal acetyltransferase domain (residues 211–401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability	-, 729696	
2.7.7.23	trimer	-	643073, 643075, 643076	
2.7.7.23	trimer	3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer)	-, 288688	
2.7.7.23	trimer	crystal structure analysis	643073	
2.7.7.23	trimer	GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein	740866	
2.7.7.23	trimer	the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein	-, 729696	
2.7.7.23	trimer	trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction	723724	
2.7.7.23	trimer	two-domain architecture of GlmU, one monomer per asymmetric unit, and a trimeric quaternary structure known for GlmU proteins	720042	
2.7.7.23	trimer	x-ray crystallography	-, 690292